A non-essential amino acid that occurs in high levels in its free state in plasma. It is produced from pyruvate by transamination. It is involved in sugar and acid metabolism, increases IMMUNITY, and provides energy for muscle tissue, BRAIN, and the CENTRAL NERVOUS SYSTEM.
An enzyme that catalyzes the conversion of L-alanine and 2-oxoglutarate to pyruvate and L-glutamate. (From Enzyme Nomenclature, 1992) EC
A pyridoxal-phosphate protein that reversibly catalyzes the conversion of L-alanine to D-alanine. EC
An interleukin-1 subtype that is synthesized as an inactive membrane-bound pro-protein. Proteolytic processing of the precursor form by CASPASE 1 results in release of the active form of interleukin-1beta from the membrane.
An 11-kDa protein associated with the outer membrane of many cells including lymphocytes. It is the small subunit of the MHC class I molecule. Association with beta 2-microglobulin is generally required for the transport of class I heavy chains from the endoplasmic reticulum to the cell surface. Beta 2-microglobulin is present in small amounts in serum, csf, and urine of normal people, and to a much greater degree in the urine and plasma of patients with tubular proteinemia, renal failure, or kidney transplants.
An NAD-dependent enzyme that catalyzes the reversible DEAMINATION of L-ALANINE to PYRUVATE and AMMONIA. The enzyme is needed for growth when ALANINE is the sole CARBON or NITROGEN source. It may also play a role in CELL WALL synthesis because L-ALANINE is an important constituent of the PEPTIDOGLYCAN layer.
One of two major pharmacologically defined classes of adrenergic receptors. The beta adrenergic receptors play an important role in regulating CARDIAC MUSCLE contraction, SMOOTH MUSCLE relaxation, and GLYCOGENOLYSIS.
An integrin beta subunit of approximately 85-kDa in size which has been found in INTEGRIN ALPHAIIB-containing and INTEGRIN ALPHAV-containing heterodimers. Integrin beta3 occurs as three alternatively spliced isoforms, designated beta3A-C.
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.
A factor synthesized in a wide variety of tissues. It acts synergistically with TGF-alpha in inducing phenotypic transformation and can also act as a negative autocrine growth factor. TGF-beta has a potential role in embryonal development, cellular differentiation, hormone secretion, and immune function. TGF-beta is found mostly as homodimer forms of separate gene products TGF-beta1, TGF-beta2 or TGF-beta3. Heterodimers composed of TGF-beta1 and 2 (TGF-beta1.2) or of TGF-beta2 and 3 (TGF-beta2.3) have been isolated. The TGF-beta proteins are synthesized as precursor proteins.
Genetically engineered MUTAGENESIS at a specific site in the DNA molecule that introduces a base substitution, or an insertion or deletion.
The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.
An integrin found in FIBROBLASTS; PLATELETS; MONOCYTES, and LYMPHOCYTES. Integrin alpha5beta1 is the classical receptor for FIBRONECTIN, but it also functions as a receptor for LAMININ and several other EXTRACELLULAR MATRIX PROTEINS.
Also known as CD104 antigen, this protein is distinguished from other beta integrins by its relatively long cytoplasmic domain (approximately 1000 amino acids vs. approximately 50). Five alternatively spliced isoforms have been described.
The parts of a macromolecule that directly participate in its specific combination with another molecule.
This intrgrin is a key component of HEMIDESMOSOMES and is required for their formation and maintenance in epithelial cells. Integrin alpha6beta4 is also found on thymocytes, fibroblasts, and Schwann cells, where it functions as a laminin receptor (RECEPTORS, LAMININ) and is involved in wound healing, cell migration, and tumor invasiveness.
Integrin beta chains combine with integrin alpha chains to form heterodimeric cell surface receptors. Integrins have traditionally been classified into functional groups based on the identity of one of three beta chains present in the heterodimer. The beta chain is necessary and sufficient for integrin-dependent signaling. Its short cytoplasmic tail contains sequences critical for inside-out signaling.
The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.
A 44-kDa highly glycosylated plasma protein that binds phospholipids including CARDIOLIPIN; APOLIPOPROTEIN E RECEPTOR; membrane phospholipids, and other anionic phospholipid-containing moieties. It plays a role in coagulation and apoptotic processes. Formerly known as apolipoprotein H, it is an autoantigen in patients with ANTIPHOSPHOLIPID ANTIBODIES.
Enzymes of the transferase class that catalyze the conversion of L-aspartate and 2-ketoglutarate to oxaloacetate and L-glutamate. EC
Established cell cultures that have the potential to propagate indefinitely.
The rate dynamics in chemical or physical systems.
The naturally occurring or experimentally induced replacement of one or more AMINO ACIDS in a protein with another. If a functionally equivalent amino acid is substituted, the protein may retain wild-type activity. Substitution may also diminish, enhance, or eliminate protein function. Experimentally induced substitution is often used to study enzyme activities and binding site properties.
Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations.
Integrin alpha4beta1 is a FIBRONECTIN and VCAM-1 receptor present on LYMPHOCYTES; MONOCYTES; EOSINOPHILS; NK CELLS and thymocytes. It is involved in both cell-cell and cell- EXTRACELLULAR MATRIX adhesion and plays a role in INFLAMMATION, hematopoietic cell homing and immune function, and has been implicated in skeletal MYOGENESIS; NEURAL CREST migration and proliferation, lymphocyte maturation and morphogenesis of the PLACENTA and HEART.
Proteins prepared by recombinant DNA technology.
Organic compounds that generally contain an amino (-NH2) and a carboxyl (-COOH) group. Twenty alpha-amino acids are the subunits which are polymerized to form proteins.
A subclass of beta-adrenergic receptors (RECEPTORS, ADRENERGIC, BETA). The adrenergic beta-2 receptors are more sensitive to EPINEPHRINE than to NOREPINEPHRINE and have a high affinity for the agonist TERBUTALINE. They are widespread, with clinically important roles in SKELETAL MUSCLE; LIVER; and vascular, bronchial, gastrointestinal, and genitourinary SMOOTH MUSCLE.
An integrin found on fibroblasts, platelets, endothelial and epithelial cells, and lymphocytes where it functions as a receptor for COLLAGEN and LAMININ. Although originally referred to as the collagen receptor, it is one of several receptors for collagen. Ligand binding to integrin alpha2beta1 triggers a cascade of intracellular signaling, including activation of p38 MAP kinase.
Cells propagated in vitro in special media conducive to their growth. Cultured cells are used to study developmental, morphologic, metabolic, physiologic, and genetic processes, among others.
Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.
A family of transmembrane glycoproteins (MEMBRANE GLYCOPROTEINS) consisting of noncovalent heterodimers. They interact with a wide variety of ligands including EXTRACELLULAR MATRIX PROTEINS; COMPLEMENT, and other cells, while their intracellular domains interact with the CYTOSKELETON. The integrins consist of at least three identified families: the cytoadhesin receptors(RECEPTORS, CYTOADHESIN), the leukocyte adhesion receptors (RECEPTORS, LEUKOCYTE ADHESION), and the VERY LATE ANTIGEN RECEPTORS. Each family contains a common beta-subunit (INTEGRIN BETA CHAINS) combined with one or more distinct alpha-subunits (INTEGRIN ALPHA CHAINS). These receptors participate in cell-matrix and cell-cell adhesion in many physiologically important processes, including embryological development; HEMOSTASIS; THROMBOSIS; WOUND HEALING; immune and nonimmune defense mechanisms; and oncogenic transformation.
Integrin beta-1 chains which are expressed as heterodimers that are noncovalently associated with specific alpha-chains of the CD49 family (CD49a-f). CD29 is expressed on resting and activated leukocytes and is a marker for all of the very late activation antigens on cells. (from: Barclay et al., The Leukocyte Antigen FactsBook, 1993, p164)
A soluble factor produced by MONOCYTES; MACROPHAGES, and other cells which activates T-lymphocytes and potentiates their response to mitogens or antigens. Interleukin-1 is a general term refers to either of the two distinct proteins, INTERLEUKIN-1ALPHA and INTERLEUKIN-1BETA. The biological effects of IL-1 include the ability to replace macrophage requirements for T-cell activation.
A cell surface receptor mediating cell adhesion to the EXTRACELLULAR MATRIX and to other cells via binding to LAMININ. It is involved in cell migration, embryonic development, leukocyte activation and tumor cell invasiveness. Integrin alpha6beta1 is the major laminin receptor on PLATELETS; LEUKOCYTES; and many EPITHELIAL CELLS, and ligand binding may activate a number of signal transduction pathways. Alternative splicing of the cytoplasmic domain of the alpha6 subunit (INTEGRIN ALPHA6) results in the formation of A and B isoforms of the heterodimer, which are expressed in a tissue-specific manner.
The introduction of a phosphoryl group into a compound through the formation of an ester bond between the compound and a phosphorus moiety.
A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances.
A subclass of beta-adrenergic receptors (RECEPTORS, ADRENERGIC, BETA). The adrenergic beta-1 receptors are equally sensitive to EPINEPHRINE and NOREPINEPHRINE and bind the agonist DOBUTAMINE and the antagonist METOPROLOL with high affinity. They are found in the HEART, juxtaglomerular cells, and in the central and peripheral nervous systems.
RNA sequences that serve as templates for protein synthesis. Bacterial mRNAs are generally primary transcripts in that they do not require post-transcriptional processing. Eukaryotic mRNA is synthesized in the nucleus and must be exported to the cytoplasm for translation. Most eukaryotic mRNAs have a sequence of polyadenylic acid at the 3' end, referred to as the poly(A) tail. The function of this tail is not known for certain, but it may play a role in the export of mature mRNA from the nucleus as well as in helping stabilize some mRNA molecules by retarding their degradation in the cytoplasm.
The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain).
A glycogen synthase kinase that was originally described as a key enzyme involved in glycogen metabolism. It regulates a diverse array of functions such as CELL DIVISION, microtubule function and APOPTOSIS.
Integrin alpha1beta1 functions as a receptor for LAMININ and COLLAGEN. It is widely expressed during development, but in the adult is the predominant laminin receptor (RECEPTORS, LAMININ) in mature SMOOTH MUSCLE CELLS, where it is important for maintenance of the differentiated phenotype of these cells. Integrin alpha1beta1 is also found in LYMPHOCYTES and microvascular endothelial cells, and may play a role in angiogenesis. In SCHWANN CELLS and neural crest cells, it is involved in cell migration. Integrin alpha1beta1 is also known as VLA-1 and CD49a-CD29.
The intracellular transfer of information (biological activation/inhibition) through a signal pathway. In each signal transduction system, an activation/inhibition signal from a biologically active molecule (hormone, neurotransmitter) is mediated via the coupling of a receptor/enzyme to a second messenger system or to an ion channel. Signal transduction plays an important role in activating cellular functions, cell differentiation, and cell proliferation. Examples of signal transduction systems are the GAMMA-AMINOBUTYRIC ACID-postsynaptic receptor-calcium ion channel system, the receptor-mediated T-cell activation pathway, and the receptor-mediated activation of phospholipases. Those coupled to membrane depolarization or intracellular release of calcium include the receptor-mediated activation of cytotoxic functions in granulocytes and the synaptic potentiation of protein kinase activation. Some signal transduction pathways may be part of larger signal transduction pathways; for example, protein kinase activation is part of the platelet activation signal pathway.
The relationship between the chemical structure of a compound and its biological or pharmacological activity. Compounds are often classed together because they have structural characteristics in common including shape, size, stereochemical arrangement, and distribution of functional groups.
The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.
The uptake of naked or purified DNA by CELLS, usually meaning the process as it occurs in eukaryotic cells. It is analogous to bacterial transformation (TRANSFORMATION, BACTERIAL) and both are routinely employed in GENE TRANSFER TECHNIQUES.
A subtype of transforming growth factor beta that is synthesized by a wide variety of cells. It is synthesized as a precursor molecule that is cleaved to form mature TGF-beta 1 and TGF-beta1 latency-associated peptide. The association of the cleavage products results in the formation a latent protein which must be activated to bind its receptor. Defects in the gene that encodes TGF-beta1 are the cause of CAMURATI-ENGELMANN SYNDROME.
One of the ESTROGEN RECEPTORS that has greater affinity for ISOFLAVONES than ESTROGEN RECEPTOR ALPHA does. There is great sequence homology with ER alpha in the DNA-binding domain but not in the ligand binding and hinge domains.
A subclass of beta-adrenergic receptors (RECEPTORS, ADRENERGIC, BETA). The beta-3 adrenergic receptors are the predominant beta-adrenergic receptor type expressed in white and brown ADIPOCYTES and are involved in modulating ENERGY METABOLISM and THERMOGENESIS.
Adherence of cells to surfaces or to other cells.
A non-essential amino acid occurring in natural form as the L-isomer. It is synthesized from GLYCINE or THREONINE. It is involved in the biosynthesis of PURINES; PYRIMIDINES; and other amino acids.
The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells.
A non-essential amino acid present abundantly throughout the body and is involved in many metabolic processes. It is synthesized from GLUTAMIC ACID and AMMONIA. It is the principal carrier of NITROGEN in the body and is an important energy source for many cells.
A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc.
Drugs that selectively bind to and activate beta-adrenergic receptors.
A subclass of enzymes of the transferase class that catalyze the transfer of an amino group from a donor (generally an amino acid) to an acceptor (generally a 2-keto acid). Most of these enzymes are pyridoxyl phosphate proteins. (Dorland, 28th ed) EC 2.6.1.
Compounds and molecular complexes that consist of very large numbers of atoms and are generally over 500 kDa in size. In biological systems macromolecular substances usually can be visualized using ELECTRON MICROSCOPY and are distinguished from ORGANELLES by the lack of a membrane structure.
Brain waves with frequency between 15-30 Hz seen on EEG during wakefulness and mental activity.
The level of protein structure in which regular hydrogen-bond interactions within contiguous stretches of polypeptide chain give rise to alpha helices, beta strands (which align to form beta sheets) or other types of coils. This is the first folding level of protein conformation.
Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques.
A DNA repair enzyme that catalyzes DNA synthesis during base excision DNA repair. EC
Recombinant proteins produced by the GENETIC TRANSLATION of fused genes formed by the combination of NUCLEIC ACID REGULATORY SEQUENCES of one or more genes with the protein coding sequences of one or more genes.
Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control (induction or repression) of gene action at the level of transcription or translation.
A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.
Single chains of amino acids that are the units of multimeric PROTEINS. Multimeric proteins can be composed of identical or non-identical subunits. One or more monomeric subunits may compose a protomer which itself is a subunit structure of a larger assembly.
Compounds bind to and activate ADRENERGIC BETA-2 RECEPTORS.
A multi-functional catenin that participates in CELL ADHESION and nuclear signaling. Beta catenin binds CADHERINS and helps link their cytoplasmic tails to the ACTIN in the CYTOSKELETON via ALPHA CATENIN. It also serves as a transcriptional co-activator and downstream component of WNT PROTEIN-mediated SIGNAL TRANSDUCTION PATHWAYS.
The relationship between the dose of an administered drug and the response of the organism to the drug.
Short sequences (generally about 10 base pairs) of DNA that are complementary to sequences of messenger RNA and allow reverse transcriptases to start copying the adjacent sequences of mRNA. Primers are used extensively in genetic and molecular biology techniques.
Elements of limited time intervals, contributing to particular results or situations.
Cell-surface proteins that bind transforming growth factor beta and trigger changes influencing the behavior of cells. Two types of transforming growth factor receptors have been recognized. They differ in affinity for different members of the transforming growth factor beta family and in cellular mechanisms of action.
A subfamily in the family MURIDAE, comprising the hamsters. Four of the more common genera are Cricetus, CRICETULUS; MESOCRICETUS; and PHODOPUS.
A non-essential amino acid. It is found primarily in gelatin and silk fibroin and used therapeutically as a nutrient. It is also a fast inhibitory neurotransmitter.
A mutation caused by the substitution of one nucleotide for another. This results in the DNA molecule having a change in a single base pair.
A molecule that binds to another molecule, used especially to refer to a small molecule that binds specifically to a larger molecule, e.g., an antigen binding to an antibody, a hormone or neurotransmitter binding to a receptor, or a substrate or allosteric effector binding to an enzyme. Ligands are also molecules that donate or accept a pair of electrons to form a coordinate covalent bond with the central metal atom of a coordination complex. (From Dorland, 27th ed)
An essential amino acid occurring naturally in the L-form, which is the active form. It is found in eggs, milk, gelatin, and other proteins.
Process of generating a genetic MUTATION. It may occur spontaneously or be induced by MUTAGENS.
The arrangement of two or more amino acid or base sequences from an organism or organisms in such a way as to align areas of the sequences sharing common properties. The degree of relatedness or homology between the sequences is predicted computationally or statistically based on weights assigned to the elements aligned between the sequences. This in turn can serve as a potential indicator of the genetic relatedness between the organisms.
The phenotypic manifestation of a gene or genes by the processes of GENETIC TRANSCRIPTION and GENETIC TRANSLATION.
Spectroscopic method of measuring the magnetic moment of elementary particles such as atomic nuclei, protons or electrons. It is employed in clinical applications such as NMR Tomography (MAGNETIC RESONANCE IMAGING).
A thiol-containing non-essential amino acid that is oxidized to form CYSTINE.
Identification of proteins or peptides that have been electrophoretically separated by blot transferring from the electrophoresis gel to strips of nitrocellulose paper, followed by labeling with antibody probes.
One of the non-essential amino acids commonly occurring in the L-form. It is found in animals and plants, especially in sugar cane and sugar beets. It may be a neurotransmitter.
The lipid- and protein-containing, selectively permeable membrane that surrounds the cytoplasm in prokaryotic and eukaryotic cells.
CELL LINES derived from the CV-1 cell line by transformation with a replication origin defective mutant of SV40 VIRUS, which codes for wild type large T antigen (ANTIGENS, POLYOMAVIRUS TRANSFORMING). They are used for transfection and cloning. (The CV-1 cell line was derived from the kidney of an adult male African green monkey (CERCOPITHECUS AETHIOPS).)
CELL LINE derived from the ovary of the Chinese hamster, Cricetulus griseus (CRICETULUS). The species is a favorite for cytogenetic studies because of its small chromosome number. The cell line has provided model systems for the study of genetic alterations in cultured mammalian cells.
A spectrum of clinical liver diseases ranging from mild biochemical abnormalities to ACUTE LIVER FAILURE, caused by drugs, drug metabolites, and chemicals from the environment.
Strains of mice in which certain GENES of their GENOMES have been disrupted, or "knocked-out". To produce knockouts, using RECOMBINANT DNA technology, the normal DNA sequence of the gene being studied is altered to prevent synthesis of a normal gene product. Cloned cells in which this DNA alteration is successful are then injected into mouse EMBRYOS to produce chimeric mice. The chimeric mice are then bred to yield a strain in which all the cells of the mouse contain the disrupted gene. Knockout mice are used as EXPERIMENTAL ANIMAL MODELS for diseases (DISEASE MODELS, ANIMAL) and to clarify the functions of the genes.
Commonly observed structural components of proteins formed by simple combinations of adjacent secondary structures. A commonly observed structure may be composed of a CONSERVED SEQUENCE which can be represented by a CONSENSUS SEQUENCE.
AMINO ALCOHOLS containing the propanolamine (NH2CH2CHOHCH2) group and its derivatives.
A deoxyribonucleotide polymer that is the primary genetic material of all cells. Eukaryotic and prokaryotic organisms normally contain DNA in a double-stranded state, yet several important biological processes transiently involve single-stranded regions. DNA, which consists of a polysugar-phosphate backbone possessing projections of purines (adenine and guanine) and pyrimidines (thymine and cytosine), forms a double helix that is held together by hydrogen bonds between these purines and pyrimidines (adenine to thymine and guanine to cytosine).
The facilitation of a chemical reaction by material (catalyst) that is not consumed by the reaction.
Conversion of an inactive form of an enzyme to one possessing metabolic activity. It includes 1, activation by ions (activators); 2, activation by cofactors (coenzymes); and 3, conversion of an enzyme precursor (proenzyme or zymogen) to an active enzyme.
Receptors such as INTEGRIN ALPHAVBETA3 that bind VITRONECTIN with high affinity and play a role in cell migration. They also bind FIBRINOGEN; VON WILLEBRAND FACTOR; osteopontin; and THROMBOSPONDINS.
The level of protein structure in which combinations of secondary protein structures (alpha helices, beta sheets, loop regions, and motifs) pack together to form folded shapes called domains. Disulfide bridges between cysteines in two different parts of the polypeptide chain along with other interactions between the chains play a role in the formation and stabilization of tertiary structure. Small proteins usually consist of only one domain but larger proteins may contain a number of domains connected by segments of polypeptide chain which lack regular secondary structure.
The biosynthesis of RNA carried out on a template of DNA. The biosynthesis of DNA from an RNA template is called REVERSE TRANSCRIPTION.
Domesticated bovine animals of the genus Bos, usually kept on a farm or ranch and used for the production of meat or dairy products or for heavy labor.
Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.
Peptides composed of between two and twelve amino acids.
A primary source of energy for living organisms. It is naturally occurring and is found in fruits and other parts of plants in its free state. It is used therapeutically in fluid and nutrient replacement.
Nucleocytoplasmic transport molecules that bind to ALPHA KARYOPHERINS in the CYTOSOL and are involved in transport of molecules through the NUCLEAR PORE COMPLEX. Once inside the CELL NUCLEUS beta karyopherins interact with RAN GTP-BINDING PROTEIN and dissociate from alpha karyopherins. Beta karyopherins bound to RAN GTP-BINDING PROTEIN are then re-transported to the cytoplasm where hydrolysis of the GTP of RAN GTP-BINDING PROTEIN causes release of karyopherin beta.
Serum glycoprotein produced by activated MACROPHAGES and other mammalian MONONUCLEAR LEUKOCYTES. It has necrotizing activity against tumor cell lines and increases ability to reject tumor transplants. Also known as TNF-alpha, it is only 30% homologous to TNF-beta (LYMPHOTOXIN), but they share TNF RECEPTORS.
A non-essential amino acid that is synthesized from GLUTAMIC ACID. It is an essential component of COLLAGEN and is important for proper functioning of joints and tendons.
The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments.
Cells grown in vitro from neoplastic tissue. If they can be established as a TUMOR CELL LINE, they can be propagated in cell culture indefinitely.
An essential branched-chain amino acid important for hemoglobin formation.
Structurally related forms of an enzyme. Each isoenzyme has the same mechanism and classification, but differs in its chemical, physical, or immunological characteristics.
A phosphoinositide phospholipase C subtype that is primarily regulated by its association with HETEROTRIMERIC G-PROTEINS. It is structurally related to PHOSPHOLIPASE C DELTA with the addition of C-terminal extension of 400 residues.
Non-antibody proteins secreted by inflammatory leukocytes and some non-leukocytic cells, that act as intercellular mediators. They differ from classical hormones in that they are produced by a number of tissue or cell types rather than by specialized glands. They generally act locally in a paracrine or autocrine rather than endocrine manner.
A strain of albino rat used widely for experimental purposes because of its calmness and ease of handling. It was developed by the Sprague-Dawley Animal Company.
Glycoproteins found on the surfaces of cells, particularly in fibrillar structures. The proteins are lost or reduced when these cells undergo viral or chemical transformation. They are highly susceptible to proteolysis and are substrates for activated blood coagulation factor VIII. The forms present in plasma are called cold-insoluble globulins.
Transport proteins that carry specific substances in the blood or across cell membranes.
Proteins which are found in membranes including cellular and intracellular membranes. They consist of two types, peripheral and integral proteins. They include most membrane-associated enzymes, antigenic proteins, transport proteins, and drug, hormone, and lectin receptors.
Single-stranded complementary DNA synthesized from an RNA template by the action of RNA-dependent DNA polymerase. cDNA (i.e., complementary DNA, not circular DNA, not C-DNA) is used in a variety of molecular cloning experiments as well as serving as a specific hybridization probe.
An essential amino acid that is required for the production of HISTAMINE.
Proteins which bind to DNA. The family includes proteins which bind to both double- and single-stranded DNA and also includes specific DNA binding proteins in serum which can be used as markers for malignant diseases.
Drugs that bind to but do not activate beta-adrenergic receptors thereby blocking the actions of beta-adrenergic agonists. Adrenergic beta-antagonists are used for treatment of hypertension, cardiac arrhythmias, angina pectoris, glaucoma, migraine headaches, and anxiety.
The study of crystal structure using X-RAY DIFFRACTION techniques. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
Different forms of a protein that may be produced from different GENES, or from the same gene by ALTERNATIVE SPLICING.
In vitro method for producing large amounts of specific DNA or RNA fragments of defined length and sequence from small amounts of short oligonucleotide flanking sequences (primers). The essential steps include thermal denaturation of the double-stranded target molecules, annealing of the primers to their complementary sequences, and extension of the annealed primers by enzymatic synthesis with DNA polymerase. The reaction is efficient, specific, and extremely sensitive. Uses for the reaction include disease diagnosis, detection of difficult-to-isolate pathogens, mutation analysis, genetic testing, DNA sequencing, and analyzing evolutionary relationships.
Extrachromosomal, usually CIRCULAR DNA molecules that are self-replicating and transferable from one organism to another. They are found in a variety of bacterial, archaeal, fungal, algal, and plant species. They are used in GENETIC ENGINEERING as CLONING VECTORS.
A variation of the PCR technique in which cDNA is made from RNA via reverse transcription. The resultant cDNA is then amplified using standard PCR protocols.
Antibodies produced by a single clone of cells.
Compounds that bind to and activate ADRENERGIC BETA-3 RECEPTORS.
An essential amino acid. It is often added to animal feed.
A forkhead transcription factor that regulates expression of metabolic GENES and is involved in EMBRYONIC DEVELOPMENT. Mutations in HNF-3beta have been associated with CONGENITAL HYPERINSULINISM.
A 51-amino acid pancreatic hormone that plays a major role in the regulation of glucose metabolism, directly by suppressing endogenous glucose production (GLYCOGENOLYSIS; GLUCONEOGENESIS) and indirectly by suppressing GLUCAGON secretion and LIPOLYSIS. Native insulin is a globular protein comprised of a zinc-coordinated hexamer. Each insulin monomer containing two chains, A (21 residues) and B (30 residues), linked by two disulfide bonds. Insulin is used as a drug to control insulin-dependent diabetes mellitus (DIABETES MELLITUS, TYPE 1).
Endogenous substances, usually proteins, which are effective in the initiation, stimulation, or termination of the genetic transcription process.
Histochemical localization of immunoreactive substances using labeled antibodies as reagents.
The normality of a solution with respect to HYDROGEN ions; H+. It is related to acidity measurements in most cases by pH = log 1/2[1/(H+)], where (H+) is the hydrogen ion concentration in gram equivalents per liter of solution. (McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed)
One of the two major classes of cholinergic receptors. Nicotinic receptors were originally distinguished by their preference for NICOTINE over MUSCARINE. They are generally divided into muscle-type and neuronal-type (previously ganglionic) based on pharmacology, and subunit composition of the receptors.
A strain of albino rat developed at the Wistar Institute that has spread widely at other institutions. This has markedly diluted the original strain.
An enzyme, sometimes called GGT, with a key role in the synthesis and degradation of GLUTATHIONE; (GSH, a tripeptide that protects cells from many toxins). It catalyzes the transfer of the gamma-glutamyl moiety to an acceptor amino acid.
Laboratory mice that have been produced from a genetically manipulated EGG or EMBRYO, MAMMALIAN.
An integrin that binds to a variety of plasma and extracellular matrix proteins containing the conserved RGD amino acid sequence and modulates cell adhesion. Integrin alphavbeta3 is highly expressed in OSTEOCLASTS where it may play role in BONE RESORPTION. It is also abundant in vascular smooth muscle and endothelial cells, and in some tumor cells, where it is involved in angiogenesis and cell migration. Although often referred to as the vitronectin receptor there is more than one receptor for vitronectin (RECEPTORS, VITRONECTIN).
A type of pancreatic cell representing about 50-80% of the islet cells. Beta cells secrete INSULIN.
A change from planar to elliptic polarization when an initially plane-polarized light wave traverses an optically active medium. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
Biosynthesis of GLUCOSE from nonhexose or non-carbohydrate precursors, such as LACTATE; PYRUVATE; ALANINE; and GLYCEROL.
Derivatives of GLUTAMIC ACID. Included under this heading are a broad variety of acid forms, salts, esters, and amides that contain the 2-aminopentanedioic acid structure.
Blood tests that are used to evaluate how well a patient's liver is working and also to help diagnose liver conditions.
The species Oryctolagus cuniculus, in the family Leporidae, order LAGOMORPHA. Rabbits are born in burrows, furless, and with eyes and ears closed. In contrast with HARES, rabbits have 22 chromosome pairs.
Proteins found in any species of bacterium.
The part of a cell that contains the CYTOSOL and small structures excluding the CELL NUCLEUS; MITOCHONDRIA; and large VACUOLES. (Glick, Glossary of Biochemistry and Molecular Biology, 1990)
The sum of the weight of all the atoms in a molecule.
The sequence of carbohydrates within POLYSACCHARIDES; GLYCOPROTEINS; and GLYCOLIPIDS.
The movement of cells from one location to another. Distinguish from CYTOKINESIS which is the process of dividing the CYTOPLASM of a cell.
An intermediate compound in the metabolism of carbohydrates, proteins, and fats. In thiamine deficiency, its oxidation is retarded and it accumulates in the tissues, especially in nervous structures. (From Stedman, 26th ed)
Theoretical representations that simulate the behavior or activity of biological processes or diseases. For disease models in living animals, DISEASE MODELS, ANIMAL is available. Biological models include the use of mathematical equations, computers, and other electronic equipment.
Compounds or agents that combine with an enzyme in such a manner as to prevent the normal substrate-enzyme combination and the catalytic reaction.
Immunologic method used for detecting or quantifying immunoreactive substances. The substance is identified by first immobilizing it by blotting onto a membrane and then tagging it with labeled antibodies.
A hepatocyte nuclear factor that is closely related to HEPATOCYTE NUCLEAR FACTOR 1-ALPHA but is only weakly expressed in the LIVER. Mutations in hepatocyte nuclear factor 1-beta are associated with renal CYSTS and MATURITY-ONSET DIABETES MELLITUS type 5.
A transfer RNA which is specific for carrying alanine to sites on the ribosomes in preparation for protein synthesis.
The region of an enzyme that interacts with its substrate to cause the enzymatic reaction.
Naturally occurring or experimentally induced animal diseases with pathological processes sufficiently similar to those of human diseases. They are used as study models for human diseases.
Isopropyl analog of EPINEPHRINE; beta-sympathomimetic that acts on the heart, bronchi, skeletal muscle, alimentary tract, etc. It is used mainly as bronchodilator and heart stimulant.
The interaction of two or more substrates or ligands with the same binding site. The displacement of one by the other is used in quantitative and selective affinity measurements.
DNA sequences which are recognized (directly or indirectly) and bound by a DNA-dependent RNA polymerase during the initiation of transcription. Highly conserved sequences within the promoter include the Pribnow box in bacteria and the TATA BOX in eukaryotes.
A non-essential amino acid naturally occurring in the L-form. Glutamic acid is the most common excitatory neurotransmitter in the CENTRAL NERVOUS SYSTEM.
A group of enzymes that catalyzes the phosphorylation of serine or threonine residues in proteins, with ATP or other nucleotides as phosphate donors.
Connective tissue cells which secrete an extracellular matrix rich in collagen and other macromolecules.
The beta subunit of human CHORIONIC GONADOTROPIN. Its structure is similar to the beta subunit of LUTEINIZING HORMONE, except for the additional 30 amino acids at the carboxy end with the associated carbohydrate residues. HCG-beta is used as a diagnostic marker for early detection of pregnancy, spontaneous abortion (ABORTION, SPONTANEOUS); ECTOPIC PREGNANCY; HYDATIDIFORM MOLE; CHORIOCARCINOMA; or DOWN SYNDROME.
A cell line derived from cultured tumor cells.
Irregular microscopic structures consisting of cords of endocrine cells that are scattered throughout the PANCREAS among the exocrine acini. Each islet is surrounded by connective tissue fibers and penetrated by a network of capillaries. There are four major cell types. The most abundant beta cells (50-80%) secrete INSULIN. Alpha cells (5-20%) secrete GLUCAGON. PP cells (10-35%) secrete PANCREATIC POLYPEPTIDE. Delta cells (~5%) secrete SOMATOSTATIN.
The process of cleaving a chemical compound by the addition of a molecule of water.
Salts or esters of LACTIC ACID containing the general formula CH3CHOHCOOR.
A species of CERCOPITHECUS containing three subspecies: C. tantalus, C. pygerythrus, and C. sabeus. They are found in the forests and savannah of Africa. The African green monkey (C. pygerythrus) is the natural host of SIMIAN IMMUNODEFICIENCY VIRUS and is used in AIDS research.
Lipid-containing polysaccharides which are endotoxins and important group-specific antigens. They are often derived from the cell wall of gram-negative bacteria and induce immunoglobulin secretion. The lipopolysaccharide molecule consists of three parts: LIPID A, core polysaccharide, and O-specific chains (O ANTIGENS). When derived from Escherichia coli, lipopolysaccharides serve as polyclonal B-cell mitogens commonly used in laboratory immunology. (From Dorland, 28th ed)
PKC beta encodes two proteins (PKCB1 and PKCBII) generated by alternative splicing of C-terminal exons. It is widely distributed with wide-ranging roles in processes such as B-cell receptor regulation, oxidative stress-induced apoptosis, androgen receptor-dependent transcriptional regulation, insulin signaling, and endothelial cell proliferation.
The commonest and widest ranging species of the clawed "frog" (Xenopus) in Africa. This species is used extensively in research. There is now a significant population in California derived from escaped laboratory animals.
Large, noncollagenous glycoprotein with antigenic properties. It is localized in the basement membrane lamina lucida and functions to bind epithelial cells to the basement membrane. Evidence suggests that the protein plays a role in tumor invasion.
The outward appearance of the individual. It is the product of interactions between genes, and between the GENOTYPE and the environment.
A positive regulatory effect on physiological processes at the molecular, cellular, or systemic level. At the molecular level, the major regulatory sites include membrane receptors, genes (GENE EXPRESSION REGULATION), mRNAs (RNA, MESSENGER), and proteins.
High energy POSITRONS or ELECTRONS ejected from a disintegrating atomic nucleus.
A branched-chain essential amino acid that has stimulant activity. It promotes muscle growth and tissue repair. It is a precursor in the penicillin biosynthetic pathway.
Cell-surface glycoprotein beta-chains that are non-covalently linked to specific alpha-chains of the CD11 family of leukocyte-adhesion molecules (RECEPTORS, LEUKOCYTE-ADHESION). A defect in the gene encoding CD18 causes LEUKOCYTE-ADHESION DEFICIENCY SYNDROME.
Peptides generated from AMYLOID BETA-PEPTIDES PRECURSOR. An amyloid fibrillar form of these peptides is the major component of amyloid plaques found in individuals with Alzheimer's disease and in aged individuals with trisomy 21 (DOWN SYNDROME). The peptide is found predominantly in the nervous system, but there have been reports of its presence in non-neural tissue.
Serologic tests in which a positive reaction manifested by visible CHEMICAL PRECIPITATION occurs when a soluble ANTIGEN reacts with its precipitins, i.e., ANTIBODIES that can form a precipitate.
Female germ cells derived from OOGONIA and termed OOCYTES when they enter MEIOSIS. The primary oocytes begin meiosis but are arrested at the diplotene state until OVULATION at PUBERTY to give rise to haploid secondary oocytes or ova (OVUM).
A TGF-beta subtype that was originally identified as a GLIOBLASTOMA-derived factor which inhibits the antigen-dependent growth of both helper and CYTOTOXIC T LYMPHOCYTES. It is synthesized as a precursor molecule that is cleaved to form mature TGF-beta2 and TGF-beta2 latency-associated peptide. The association of the cleavage products results in the formation a latent protein which must be activated to bind its receptor.
Body organ that filters blood for the secretion of URINE and that regulates ion concentrations.
Linear POLYPEPTIDES that are synthesized on RIBOSOMES and may be further modified, crosslinked, cleaved, or assembled into complex proteins with several subunits. The specific sequence of AMINO ACIDS determines the shape the polypeptide will take, during PROTEIN FOLDING, and the function of the protein.
One of the mechanisms by which CELL DEATH occurs (compare with NECROSIS and AUTOPHAGOCYTOSIS). Apoptosis is the mechanism responsible for the physiological deletion of cells and appears to be intrinsically programmed. It is characterized by distinctive morphologic changes in the nucleus and cytoplasm, chromatin cleavage at regularly spaced sites, and the endonucleolytic cleavage of genomic DNA; (DNA FRAGMENTATION); at internucleosomal sites. This mode of cell death serves as a balance to mitosis in regulating the size of animal tissues and in mediating pathologic processes associated with tumor growth.
A negative regulatory effect on physiological processes at the molecular, cellular, or systemic level. At the molecular level, the major regulatory sites include membrane receptors, genes (GENE EXPRESSION REGULATION), mRNAs (RNA, MESSENGER), and proteins.
The movement of materials (including biochemical substances and drugs) through a biological system at the cellular level. The transport can be across cell membranes and epithelial layers. It also can occur within intracellular compartments and extracellular compartments.
Regulatory proteins that act as molecular switches. They control a wide range of biological processes including: receptor signaling, intracellular signal transduction pathways, and protein synthesis. Their activity is regulated by factors that control their ability to bind to and hydrolyze GTP to GDP. EC 3.6.1.-.
The process of moving proteins from one cellular compartment (including extracellular) to another by various sorting and transport mechanisms such as gated transport, protein translocation, and vesicular transport.
Liquid chromatographic techniques which feature high inlet pressures, high sensitivity, and high speed.
A long pro-domain caspase that has specificity for the precursor form of INTERLEUKIN-1BETA. It plays a role in INFLAMMATION by catalytically converting the inactive forms of CYTOKINES such as interleukin-1beta to their active, secreted form. Caspase 1 is referred as interleukin-1beta converting enzyme and is frequently abbreviated ICE.
An essential aromatic amino acid that is a precursor of MELANIN; DOPAMINE; noradrenalin (NOREPINEPHRINE), and THYROXINE.
A colorless alkaline gas. It is formed in the body during decomposition of organic materials during a large number of metabolically important reactions. Note that the aqueous form of ammonia is referred to as AMMONIUM HYDROXIDE.
Differentiation antigens residing on mammalian leukocytes. CD stands for cluster of differentiation, which refers to groups of monoclonal antibodies that show similar reactivity with certain subpopulations of antigens of a particular lineage or differentiation stage. The subpopulations of antigens are also known by the same CD designation.
An adenine nucleotide containing three phosphate groups esterified to the sugar moiety. In addition to its crucial roles in metabolism adenosine triphosphate is a neurotransmitter.
A cytokine that stimulates the growth and differentiation of B-LYMPHOCYTES and is also a growth factor for HYBRIDOMAS and plasmacytomas. It is produced by many different cells including T-LYMPHOCYTES; MONOCYTES; and FIBROBLASTS.
Members of the class of compounds composed of AMINO ACIDS joined together by peptide bonds between adjacent amino acids into linear, branched or cyclical structures. OLIGOPEPTIDES are composed of approximately 2-12 amino acids. Polypeptides are composed of approximately 13 or more amino acids. PROTEINS are linear polypeptides that are normally synthesized on RIBOSOMES.
A non-essential amino acid that is involved in the metabolic control of cell functions in nerve and brain tissue. It is biosynthesized from ASPARTIC ACID and AMMONIA by asparagine synthetase. (From Concise Encyclopedia Biochemistry and Molecular Biology, 3rd ed)
Progressive restriction of the developmental potential and increasing specialization of function that leads to the formation of specialized cells, tissues, and organs.
Proteins produced from GENES that have acquired MUTATIONS.
The fission of a CELL. It includes CYTOKINESIS, when the CYTOPLASM of a cell is divided, and CELL NUCLEUS DIVISION.
Technique using an instrument system for making, processing, and displaying one or more measurements on individual cells obtained from a cell suspension. Cells are usually stained with one or more fluorescent dyes specific to cell components of interest, e.g., DNA, and fluorescence of each cell is measured as it rapidly transverses the excitation beam (laser or mercury arc lamp). Fluorescence provides a quantitative measure of various biochemical and biophysical properties of the cell, as well as a basis for cell sorting. Other measurable optical parameters include light absorption and light scattering, the latter being applicable to the measurement of cell size, shape, density, granularity, and stain uptake.
The part of CENTRAL NERVOUS SYSTEM that is contained within the skull (CRANIUM). Arising from the NEURAL TUBE, the embryonic brain is comprised of three major parts including PROSENCEPHALON (the forebrain); MESENCEPHALON (the midbrain); and RHOMBENCEPHALON (the hindbrain). The developed brain consists of CEREBRUM; CEREBELLUM; and other structures in the BRAIN STEM.

Analysis of 4-phosphopantetheinylation of polyhydroxybutyrate synthase from Ralstonia eutropha: generation of beta-alanine auxotrophic Tn5 mutants and cloning of the panD gene region. (1/407)

The postulated posttranslational modification of the polyhydroxybutyrate (PHA) synthase from Ralstonia eutropha by 4-phosphopantetheine was investigated. Four beta-alanine auxotrophic Tn5-induced mutants of R. eutropha HF39 were isolated, and two insertions were mapped in an open reading frame with strong similarity to the panD gene from Escherichia coli, encoding L-aspartate-1-decarboxylase (EC, whereas two other insertions were mapped in an open reading frame (ORF) with strong similarity to the NAD(P)+ transhydrogenase (EC alpha 1 subunit, encoded by the pntAA gene from Escherichia coli. The panD gene was cloned by complementation of the panD mutant of R. eutropha Q20. DNA sequencing of the panD gene region (3,312 bp) revealed an ORF of 365 bp, encoding a protein with 63 and 67% amino acid sequence similarity to PanD from E. coli and Bacillus subtilis, respectively. Subcloning of only this ORF into vectors pBBR1MCS-3 and pBluescript KS- led to complementation of the panD mutants of R. eutropha and E. coli SJ16, respectively. panD-encoded L-aspartate-1-decarboxylase was further confirmed by an enzymatic assay. Upstream of panD, an ORF with strong similarity to pntAA from E. coli, encoding NAD(P)+ transhydrogenase subunit alpha 1 was found; downstream of panD, two ORFs with strong similarity to pntAB and pntB, encoding subunits alpha 2 and beta of the NAD(P)+ transhydrogenase, respectively, were identified. Thus, a hitherto undetermined organization of pan and pnt genes was found in R. eutropha. Labeling experiments using one of the R. eutropha panD mutants and [2-14C]beta-alanine provided no evidence that R. eutropha PHA synthase is covalently modified by posttranslational attachment of 4-phosphopantetheine, nor did the E. coli panD mutant exhibit detectable labeling of functional PHA synthase from R. eutropha.  (+info)

H+-zwitterionic amino acid symport at the brush-border membrane of human intestinal epithelial (CACO-2) cells. (2/407)

Transport of a number of dipolar amino acids (and the orally active antibiotic D-cycloserine) across the apical membrane of human intestinal epithelial (Caco-2) cell monolayers is mediated by a Na+-independent, pH-dependent transport mechanism. Relatively little is known about the mode of action of this transport system so to differentiate between pH dependence and proton coupling three experimental protocols were designed and tested. The results demonstrate, firstly, that it is the transapical pH gradient and its maintenance (rather than apical acidity alone) that is important in amino acid uptake. Secondly, Na+-independent uptake of seven dipolar amino acids (with pKa (-log of acid dissociation constant) values between 1 50 and 4 23) showed a similar dependence on apical pH (half-maximal uptake being observed at pH 5 99-6 20). Thirdly, the pattern of pH-dependent amino acid ([beta]-alanine) uptake is similar irrespective of whether the cationic substrate concentration is varied or constant, demonstrating no relationship between uptake and concentration of the cationic form of the amino acid. These observations demonstrate that the transport mechanism is a H+-zwitterionic amino acid symporter and suggest that the presence of a H+ gradient at the apical surface of the human small intestine (in the form of the acid microclimate) may be important in driving nutrient absorption.  (+info)

Decreased insulin-stimulated GLUT-4 translocation in glycogen-supercompensated muscles of exercised rats. (3/407)

It was recently found that the effect of an exercise-induced increase in muscle GLUT-4 on insulin-stimulated glucose transport is masked by a decreased responsiveness to insulin in glycogen-supercompensated muscle. We evaluated the role of hexosamines in this decrease in insulin responsiveness and found that UDP-N-acetyl hexosamine concentrations were not higher in glycogen-supercompensated muscles than in control muscles with a low glycogen content. We determined whether the smaller increase in glucose transport is due to translocation of fewer GLUT-4 to the cell surface with the 2-N-4-(1-azi-2,2,2-trifluroethyl)-benzoyl-1, 3-bis(D-mannose-4-yloxy)-2-propylamine (ATB-[2-3H]BMPA) photolabeling technique. The insulin-induced increase in GLUT-4 at the cell surface was no greater in glycogen-supercompensated exercised muscle than in muscles of sedentary controls and only 50% as great as in exercised muscles with a low glycogen content. We conclude that the decreased insulin responsiveness of glucose transport in glycogen-supercompensated muscle is not due to increased accumulation of hexosamine biosynthetic pathway end products and that the smaller increase in glucose transport is mediated by translocation of fewer GLUT-4 to the cell surface.  (+info)

Alterations of intratumoral pharmacokinetics of 5-fluorouracil in head and neck carcinoma during simultaneous radiochemotherapy. (4/407)

The kinetics of local drug uptake and metabolism of the anticancer drug 5-fluorouracil (5-FU) has been monitored by means of 19F nuclear magnetic resonance spectroscopy in 17 patients with neck tumors during concurrent radiochemotherapy. All of the patients underwent an accelerated hyperfractionated, concomitant-boost radiochemotherapy with 5-FU [600 or 1000 mg/m2 of body surface (b.s.)] and carboplatin (70 mg/m2 of b.s.). Serial 19F nuclear magnetic resonance spectra were obtained during and after the administration of 5-FU in a 15-T scanner with the use of a 5-cm diameter surface coil positioned on a cervical lymph node metastasis. Examinations were performed at day 1 of therapy and, in 13 patients, also after 43.5 Gy of irradiation at day 1 of the second chemotherapy cycle. Resonances of 5-FU and the catabolites 5,6-dihydro-5-fluorouracil (DHFU) and alpha-fluoro-beta-alanine (FBAL) were resolved in the tumor spectra. The median of the 5-FU and FBAL levels was significantly higher (more than 2-fold) at the second compared with the first examination, whereas the level of DHFU did not change. This effect could indicate an increased delivery of 5-FU into the interstitial space of the tumor in the course of the combined treatment, which would result in an enhanced exposure of the tumor cells to the drug. A potential mechanism for synergy between radio- and chemotherapy is discussed, but alternative mechanisms are also being considered. The findings indicate that a method is available to rationally address the design of dosing schedules in concurrent therapy regimens.  (+info)

Role of tyrosine 265 of alanine racemase from Bacillus stearothermophilus. (5/407)

Tyrosine 265 (Y265) of Bacillus stearothermophilus is believed to serve as a catalytic base specific to the L-enantiomer of a substrate amino acid by removing (or returning) an alpha-hydrogen from (or to) the isomer on the basis of the X-ray structure of the enzyme [Stamper, C.G., Morollo, A.A., and Ringe, D. (1998) Biochemistry 37, 10438-10443]. We found that the Y265-->Ala mutant (Y265A) enzyme is virtually inactive as a catalyst for alanine racemization. We examined the role of Y265 further with beta-chloroalanine as a substrate with the expectation that the Y265A mutant only catalyzes the alpha,beta-elimination of the D-enantiomer of beta-chloroalanine. However, L-beta-chloroalanine also served as a substrate; this enantiomer was rather better as a substrate than its antipode. Moreover, the mutant enzyme was as equally active as the wild-type enzyme in the elimination reaction. These findings indicate that Y265 is essential for alanine racemization but not for beta-chloroalanine elimination.  (+info)

Effect of hypertonic stress on amino acid levels and system A activity in rat peritoneal mesothelial cells. (6/407)

OBJECTIVE: Peritoneal mesothelial cells (PMC) are exposed to a hypertonic environment during peritoneal dialysis. When exposed to a hypertonic medium, many types of cells accumulate small osmotically active organic solutes, which are called osmolytes, to match the higher external osmolality. However, no information has been available concerning the osmolytes in PMC. To investigate osmoregulation in rat PMC, the levels of amino acids in the cells and the activity of system A, a major neutral amino acid transport, were measured after switching to a medium made hypertonic by the addition of NaCl. System A was measured by Na+-dependent [14C]-2-methylamino-isobutyric acid (MeAIB) uptake. RESULTS: Total amount of 20 amino acids increased from 306 to 757 nmol/mg protein after 12 hours of hypertonicity. The amount of neutral amino acids accounted for 81% of the increase in total amino acids. Glutamine, alanine, glycine, threonine, and serine were the major neutral amino acids that accumulated in the hypertonic mesothelial cells. The amount of neutral amino acids increased 2.9-fold after 12 hr of hypertonicity, and decreased thereafter. MeAIB uptake increased 36-fold relative to the uptake in isotonic cells after 4-8 hr of hypertonicity. When the culture medium was made hypertonic by adding raffinose or glucose, the activity of system A was also stimulated (raffinose > glucose > NaCl). System A was located on both the apical and basal sides of isotonic PMC, and extracellular hypertonicity stimulated the MeAIB uptake on both sides. CONCLUSIONS: These data indicate that neutral amino acids and system A transport play an important role in early-phase osmoregulation in rat peritoneal mesothelial cells.  (+info)

Fibrinogen receptor antagonist-induced thrombocytopenia in chimpanzee and rhesus monkey associated with preexisting drug-dependent antibodies to platelet glycoprotein IIb/IIIa. (7/407)

Most clinical trials with fibrinogen receptor antagonists (FRAs) have been associated with thrombocytopenia. This report describes the occurrence of thrombocytopenia in one chimpanzee and one rhesus monkey upon administration of potent FRAs. Chimpanzee A-264 experienced profound thrombocytopenia on two occasions immediately upon intravenous administration of two different potent FRAs, L-738, 167 and L-739,758. However, an equally efficacious antiaggregatory dose of another potent antagonist, L-734,217, caused no change in platelet count. These compounds did not affect platelet count in five other chimpanzees or numerous other nonhuman primates. Flow cytometric analysis showed drug-dependent antibodies (DDAbs) in the plasma of chimpanzee A-264 that bound to platelets of chimpanzees, humans, and all other primates tested only in the presence of the compounds that induced thrombocytopenia. Rhesus monkey 94-R021 experienced thrombocytopenia upon administration of a different antagonist, L-767,679, and several prodrugs that are converted into the active form, L-767,679, in the blood. More than 20 other FRAs, including those that induced thrombocytopenia in chimpanzee A-264, had no effect on platelet count in this monkey. Flow cytometric measurements again identified DDAbs that reacted with platelets of all primates tested and required the presence of L-767,679. Screening for DDAbs in the plasma of 1,032 human subjects with L-738, 167 and L-739,758 demonstrated that the incidence of these preexisting antibodies in this population was 0.8% +/- 0.6% and 1.1% +/- 0.6%, respectively.  (+info)

Investigation of the alpha(1)-glycine receptor channel-opening kinetics in the submillisecond time domain. (8/407)

The activation and desensitization kinetics of the human alpha(1)-homooligomeric glycine receptor, which was transiently expressed in HEK 293 cells, were studied with a 100-microseconds time resolution to determine the rate and equilibrium constants of individual receptor reaction steps. Concentration jumps of the activating ligands glycine and beta-alanine were initiated by photolysis of caged, inactive precursors and were followed by neurotransmitter binding, receptor-channel opening, and receptor desensitization steps that were separated along the time axis. Analysis of the ligand concentration-dependence of these processes allows the determination of 1) the rate constants of glycine binding, k(+1) approximately 10(7) M(-1) s(-1), and dissociation, k(-1) = 1900 s(-1); 2) the rates of receptor-channel opening, k(op) = 2200 s(-1), and closing, k(cl) = 38 s(-1); 3) the receptor desensitization rate, alpha = 0.45 s(-1); 4) the number of occupied ligand binding sites necessary for receptor-channel activation and desensitization, n >/= 3; and 5) the maximum receptor-channel open probability, p(0) > 0.95. The kinetics of receptor-channel activation are insensitive to the transmembrane potential. A general model for glycine receptor activation explaining the experimental data consists of a sequential mechanism based on rapid ligand-binding steps preceding a rate-limiting receptor-channel opening reaction and slow receptor desensitization.  (+info)

The definition of DILI has been revised several times over the years, but the most recent definition was published in 2013 by the International Consortium for DILI Research (ICDCR). According to this definition, DILI is defined as:

"A clinically significant alteration in liver function that is caused by a medication or other exogenous substance, and is not related to underlying liver disease. The alteration may be biochemical, morphological, or both, and may be acute or chronic."

The ICDCR definition includes several key features of DILI, including:

1. Clinically significant alteration in liver function: This means that the liver damage must be severe enough to cause symptoms or signs of liver dysfunction, such as jaundice, nausea, vomiting, or abdominal pain.
2. Caused by a medication or other exogenous substance: DILI is triggered by exposure to certain drugs or substances that are not related to underlying liver disease.
3. Not related to underlying liver disease: This means that the liver damage must not be caused by an underlying condition such as hepatitis B or C, alcoholic liver disease, or other genetic or metabolic disorders.
4. May be acute or chronic: DILI can occur as a sudden and severe injury (acute DILI) or as a slower and more insidious process (chronic DILI).

The ICDCR definition provides a standardized way of defining and diagnosing DILI, which is important for clinicians and researchers to better understand the cause of liver damage in patients who are taking medications. It also helps to identify the drugs or substances that are most likely to cause liver injury and to develop strategies for preventing or treating DILI.

1) They share similarities with humans: Many animal species share similar biological and physiological characteristics with humans, making them useful for studying human diseases. For example, mice and rats are often used to study diseases such as diabetes, heart disease, and cancer because they have similar metabolic and cardiovascular systems to humans.

2) They can be genetically manipulated: Animal disease models can be genetically engineered to develop specific diseases or to model human genetic disorders. This allows researchers to study the progression of the disease and test potential treatments in a controlled environment.

3) They can be used to test drugs and therapies: Before new drugs or therapies are tested in humans, they are often first tested in animal models of disease. This allows researchers to assess the safety and efficacy of the treatment before moving on to human clinical trials.

4) They can provide insights into disease mechanisms: Studying disease models in animals can provide valuable insights into the underlying mechanisms of a particular disease. This information can then be used to develop new treatments or improve existing ones.

5) Reduces the need for human testing: Using animal disease models reduces the need for human testing, which can be time-consuming, expensive, and ethically challenging. However, it is important to note that animal models are not perfect substitutes for human subjects, and results obtained from animal studies may not always translate to humans.

6) They can be used to study infectious diseases: Animal disease models can be used to study infectious diseases such as HIV, TB, and malaria. These models allow researchers to understand how the disease is transmitted, how it progresses, and how it responds to treatment.

7) They can be used to study complex diseases: Animal disease models can be used to study complex diseases such as cancer, diabetes, and heart disease. These models allow researchers to understand the underlying mechanisms of the disease and test potential treatments.

8) They are cost-effective: Animal disease models are often less expensive than human clinical trials, making them a cost-effective way to conduct research.

9) They can be used to study drug delivery: Animal disease models can be used to study drug delivery and pharmacokinetics, which is important for developing new drugs and drug delivery systems.

10) They can be used to study aging: Animal disease models can be used to study the aging process and age-related diseases such as Alzheimer's and Parkinson's. This allows researchers to understand how aging contributes to disease and develop potential treatments.

There are many different types of liver diseases, including:

1. Alcoholic liver disease (ALD): A condition caused by excessive alcohol consumption that can lead to inflammation, scarring, and cirrhosis.
2. Viral hepatitis: Hepatitis A, B, and C are viral infections that can cause inflammation and damage to the liver.
3. Non-alcoholic fatty liver disease (NAFLD): A condition where there is an accumulation of fat in the liver, which can lead to inflammation and scarring.
4. Cirrhosis: A condition where the liver becomes scarred and cannot function properly.
5. Hemochromatosis: A genetic disorder that causes the body to absorb too much iron, which can damage the liver and other organs.
6. Wilson's disease: A rare genetic disorder that causes copper to accumulate in the liver and brain, leading to damage and scarring.
7. Liver cancer (hepatocellular carcinoma): Cancer that develops in the liver, often as a result of cirrhosis or viral hepatitis.

Symptoms of liver disease can include fatigue, loss of appetite, nausea, abdominal pain, dark urine, pale stools, and swelling in the legs. Treatment options for liver disease depend on the underlying cause and may include lifestyle changes, medication, or surgery. In severe cases, a liver transplant may be necessary.

Prevention of liver disease includes maintaining a healthy diet and lifestyle, avoiding excessive alcohol consumption, getting vaccinated against hepatitis A and B, and managing underlying medical conditions such as obesity and diabetes. Early detection and treatment of liver disease can help to prevent long-term damage and improve outcomes for patients.

There are several key features of inflammation:

1. Increased blood flow: Blood vessels in the affected area dilate, allowing more blood to flow into the tissue and bringing with it immune cells, nutrients, and other signaling molecules.
2. Leukocyte migration: White blood cells, such as neutrophils and monocytes, migrate towards the site of inflammation in response to chemical signals.
3. Release of mediators: Inflammatory mediators, such as cytokines and chemokines, are released by immune cells and other cells in the affected tissue. These molecules help to coordinate the immune response and attract more immune cells to the site of inflammation.
4. Activation of immune cells: Immune cells, such as macrophages and T cells, become activated and start to phagocytose (engulf) pathogens or damaged tissue.
5. Increased heat production: Inflammation can cause an increase in metabolic activity in the affected tissue, leading to increased heat production.
6. Redness and swelling: Increased blood flow and leakiness of blood vessels can cause redness and swelling in the affected area.
7. Pain: Inflammation can cause pain through the activation of nociceptors (pain-sensing neurons) and the release of pro-inflammatory mediators.

Inflammation can be acute or chronic. Acute inflammation is a short-term response to injury or infection, which helps to resolve the issue quickly. Chronic inflammation is a long-term response that can cause ongoing damage and diseases such as arthritis, asthma, and cancer.

There are several types of inflammation, including:

1. Acute inflammation: A short-term response to injury or infection.
2. Chronic inflammation: A long-term response that can cause ongoing damage and diseases.
3. Autoimmune inflammation: An inappropriate immune response against the body's own tissues.
4. Allergic inflammation: An immune response to a harmless substance, such as pollen or dust mites.
5. Parasitic inflammation: An immune response to parasites, such as worms or fungi.
6. Bacterial inflammation: An immune response to bacteria.
7. Viral inflammation: An immune response to viruses.
8. Fungal inflammation: An immune response to fungi.

There are several ways to reduce inflammation, including:

1. Medications such as nonsteroidal anti-inflammatory drugs (NSAIDs), corticosteroids, and disease-modifying anti-rheumatic drugs (DMARDs).
2. Lifestyle changes, such as a healthy diet, regular exercise, stress management, and getting enough sleep.
3. Alternative therapies, such as acupuncture, herbal supplements, and mind-body practices.
4. Addressing underlying conditions, such as hormonal imbalances, gut health issues, and chronic infections.
5. Using anti-inflammatory compounds found in certain foods, such as omega-3 fatty acids, turmeric, and ginger.

It's important to note that chronic inflammation can lead to a range of health problems, including:

1. Arthritis
2. Diabetes
3. Heart disease
4. Cancer
5. Alzheimer's disease
6. Parkinson's disease
7. Autoimmune disorders, such as lupus and rheumatoid arthritis.

Therefore, it's important to manage inflammation effectively to prevent these complications and improve overall health and well-being.

There are two main types of fatty liver disease:

1. Alcoholic fatty liver disease (AFLD): This type of fatty liver disease is caused by excessive alcohol consumption and is the most common cause of fatty liver disease in the United States.
2. Non-alcoholic fatty liver disease (NAFLD): This type of fatty liver disease is not caused by alcohol consumption and is the most common cause of fatty liver disease worldwide. It is often associated with obesity, diabetes, and high cholesterol.

There are several risk factors for developing fatty liver disease, including:

* Obesity
* Physical inactivity
* High calorie intake
* Alcohol consumption
* Diabetes
* High cholesterol
* High triglycerides
* History of liver disease

Symptoms of fatty liver disease can include:

* Fatigue
* Abdominal discomfort
* Loss of appetite
* Nausea and vomiting
* Abnormal liver function tests

Diagnosis of fatty liver disease is typically made through a combination of physical examination, medical history, and diagnostic tests such as:

* Liver biopsy
* Imaging studies (ultrasound, CT or MRI scans)
* Blood tests (lipid profile, glucose, insulin, and liver function tests)

Treatment of fatty liver disease depends on the underlying cause and severity of the condition. Lifestyle modifications such as weight loss, exercise, and a healthy diet can help improve the condition. In severe cases, medications such as antioxidants, fibric acids, and anti-inflammatory drugs may be prescribed. In some cases, surgery or other procedures may be necessary.

Prevention of fatty liver disease includes:

* Maintaining a healthy weight
* Eating a balanced diet low in sugar and saturated fats
* Engaging in regular physical activity
* Limiting alcohol consumption
* Managing underlying medical conditions such as diabetes and high cholesterol.

The excessive production of oxalate can cause a range of symptoms, including kidney stones, damage to the kidneys and other organs, and an increased risk of certain infections. If left untreated, primary hyperoxaluria can lead to serious health problems and may even be fatal.

The exact cause of primary hyperoxaluria is not fully understood, but it is thought to be related to mutations in genes that code for enzymes involved in the production of oxalate. These mutations can be inherited from one or both parents, and the disorder can affect individuals of all ages and backgrounds.

There is currently no cure for primary hyperoxaluria, but various treatments are available to help manage the symptoms and prevent complications. These may include medications to reduce the production of oxalate, dietary changes to limit the intake of oxalate-rich foods, and other supportive measures to help maintain kidney function and overall health.

In summary, primary hyperoxaluria is a rare genetic disorder that affects the liver and causes an excessive amount of oxalate to be produced in the body. This can lead to a range of symptoms and health problems if left untreated, so it is important for individuals with this condition to receive prompt and appropriate medical attention.

There are two main types of thalassemia: alpha-thalassemia and beta-thalassemia. Alpha-thalassemia is caused by abnormalities in the production of the alpha-globin chain, which is one of the two chains that make up hemoglobin. Beta-thalassemia is caused by abnormalities in the production of the beta-globin chain.

Thalassemia can cause a range of symptoms, including anemia, fatigue, pale skin, and shortness of breath. In severe cases, it can lead to life-threatening complications such as heart failure, liver failure, and bone deformities. Thalassemia is usually diagnosed through blood tests that measure the levels of hemoglobin and other proteins in the blood.

There is no cure for thalassemia, but treatment can help manage the symptoms and prevent complications. Treatment may include blood transfusions, folic acid supplements, and medications to reduce the severity of anemia. In some cases, bone marrow transplantation may be recommended.

Preventive measures for thalassemia include genetic counseling and testing for individuals who are at risk of inheriting the disorder. Prenatal testing is also available for pregnant women who are carriers of the disorder. In addition, individuals with thalassemia should avoid marriage within their own family or community to reduce the risk of passing on the disorder to their children.

Overall, thalassemia is a serious and inherited blood disorder that can have significant health implications if left untreated. However, with proper treatment and management, individuals with thalassemia can lead fulfilling lives and minimize the risk of complications.

The condition can be caused by a variety of factors, including excessive alcohol consumption, viral hepatitis, non-alcoholic fatty liver disease, and certain medications. It can also be a complication of other diseases such as hemochromatosis and Wilson's disease.

The symptoms of liver cirrhosis can vary depending on the severity of the disease, but may include fatigue, loss of appetite, nausea, abdominal swelling, and pain in the upper right side of the abdomen. As the disease progresses, it can lead to complications such as esophageal varices, ascites, and liver failure, which can be life-threatening.

There is no cure for liver cirrhosis, but treatment options are available to manage the symptoms and slow the progression of the disease. These may include medications to control swelling and pain, dietary changes, and in severe cases, liver transplantation. In some cases, a liver transplant may be necessary if the disease has caused significant damage and there is no other option to save the patient's life.

In conclusion, liver cirrhosis is a serious and potentially life-threatening condition that can cause significant damage to the liver and lead to complications such as liver failure. It is important for individuals to be aware of the risk factors and symptoms of the disease in order to seek medical attention if they suspect they may have liver cirrhosis. With proper treatment and management, it is possible to slow the progression of the disease and improve the patient's quality of life.

A persistent infection with the hepatitis B virus (HBV) that can lead to liver cirrhosis and hepatocellular carcinoma. HBV is a bloodborne pathogen and can be spread through contact with infected blood, sexual contact, or vertical transmission from mother to child during childbirth.

Chronic hepatitis B is characterized by the presence of HBsAg in the blood for more than 6 months, indicating that the virus is still present in the liver. The disease can be asymptomatic or symptomatic, with symptoms such as fatigue, malaise, loss of appetite, nausea, vomiting, joint pain, and jaundice.

Chronic hepatitis B is diagnosed through serological tests such as HBsAg, anti-HBc, and HBV DNA. Treatment options include interferon alpha and nucleos(t)ide analogues, which can slow the progression of the disease but do not cure it.

Prevention strategies for chronic hepatitis B include vaccination with hepatitis B vaccine, which is effective in preventing acute and chronic HBV infection, as well as avoidance of risky behaviors such as unprotected sex and sharing of needles.

Starvation is a condition where an individual's body does not receive enough nutrients to maintain proper bodily functions and growth. It can be caused by a lack of access to food, poverty, poor nutrition, or other factors that prevent the intake of sufficient calories and essential nutrients. Starvation can lead to severe health consequences, including weight loss, weakness, fatigue, and even death.

Types of Starvation:

There are several types of starvation, each with different causes and effects. These include:

1. Acute starvation: This occurs when an individual suddenly stops eating or has a limited access to food for a short period of time.
2. Chronic starvation: This occurs when an individual consistently does not consume enough calories and nutrients over a longer period of time, leading to gradual weight loss and other health problems.
3. Malnutrition starvation: This occurs when an individual's diet is deficient in essential nutrients, leading to malnutrition and other health problems.
4. Marasmus: This is a severe form of starvation that occurs in children, characterized by extreme weight loss, weakness, and wasting of muscles and organs.
5. Kwashiorkor: This is a form of malnutrition caused by a diet lacking in protein, leading to edema, diarrhea, and other health problems.

Effects of Starvation on the Body:

Starvation can have severe effects on the body, including:

1. Weight loss: Starvation causes weight loss, which can lead to a decrease in muscle mass and a loss of essential nutrients.
2. Fatigue: Starvation can cause fatigue, weakness, and a lack of energy, making it difficult to perform daily activities.
3. Weakened immune system: Starvation can weaken the immune system, making an individual more susceptible to illnesses and infections.
4. Nutrient deficiencies: Starvation can lead to a deficiency of essential nutrients, including vitamins and minerals, which can cause a range of health problems.
5. Increased risk of disease: Starvation can increase the risk of diseases such as tuberculosis, pellagra, and other infections.
6. Mental health issues: Starvation can lead to mental health issues such as depression, anxiety, and irritability.
7. Reproductive problems: Starvation can cause reproductive problems, including infertility and miscarriage.
8. Hair loss: Starvation can cause hair loss, which can be a sign of malnutrition.
9. Skin problems: Starvation can cause skin problems, such as dryness, irritation, and infections.
10. Increased risk of death: Starvation can lead to increased risk of death, especially in children and the elderly.

It is important to note that these effects can be reversed with proper nutrition and care. If you or someone you know is experiencing starvation, it is essential to seek medical attention immediately.

The symptoms of Alzheimer's disease can vary from person to person and may progress slowly over time. Early symptoms may include memory loss, confusion, and difficulty with problem-solving. As the disease progresses, individuals may experience language difficulties, visual hallucinations, and changes in mood and behavior.

There is currently no cure for Alzheimer's disease, but there are several medications and therapies that can help manage its symptoms and slow its progression. These include cholinesterase inhibitors, memantine, and non-pharmacological interventions such as cognitive training and behavioral therapy.

Alzheimer's disease is a significant public health concern, affecting an estimated 5.8 million Americans in 2020. It is the sixth leading cause of death in the United States, and its prevalence is expected to continue to increase as the population ages.

There is ongoing research into the causes and potential treatments for Alzheimer's disease, including studies into the role of inflammation, oxidative stress, and the immune system. Other areas of research include the development of biomarkers for early detection and the use of advanced imaging techniques to monitor progression of the disease.

Overall, Alzheimer's disease is a complex and multifactorial disorder that poses significant challenges for individuals, families, and healthcare systems. However, with ongoing research and advances in medical technology, there is hope for improving diagnosis and treatment options in the future.

Reperfusion injury can cause inflammation, cell death, and impaired function in the affected tissue or organ. The severity of reperfusion injury can vary depending on the duration and severity of the initial ischemic event, as well as the promptness and effectiveness of treatment to restore blood flow.

Reperfusion injury can be a complicating factor in various medical conditions, including:

1. Myocardial infarction (heart attack): Reperfusion injury can occur when blood flow is restored to the heart muscle after a heart attack, leading to inflammation and cell death.
2. Stroke: Reperfusion injury can occur when blood flow is restored to the brain after an ischemic stroke, leading to inflammation and damage to brain tissue.
3. Organ transplantation: Reperfusion injury can occur when a transplanted organ is subjected to ischemia during harvesting or preservation, and then reperfused with blood.
4. Peripheral arterial disease: Reperfusion injury can occur when blood flow is restored to a previously occluded peripheral artery, leading to inflammation and damage to the affected tissue.

Treatment of reperfusion injury often involves medications to reduce inflammation and oxidative stress, as well as supportive care to manage symptoms and prevent further complications. In some cases, experimental therapies such as stem cell transplantation or gene therapy may be used to promote tissue repair and regeneration.

The symptoms of chronic hepatitis C may be mild or absent, but some people experience fatigue, joint pain, muscle aches, nausea, loss of appetite, and jaundice (yellowing of the skin and eyes).

Chronic hepatitis C is usually diagnosed through blood tests that detect the presence of antibodies against HCV or the virus itself. Imaging tests such as ultrasound and liver biopsy may also be performed to assess the extent of liver damage.

Treatment for chronic hepatitis C typically involves a combination of medications, including interferon and ribavirin, which can help clear the virus from the body. In severe cases, a liver transplant may be necessary. Prevention of the spread of HCV includes avoiding sharing of needles or other sharp objects, practicing safe sex, and getting tested for the virus before donating blood or organs.

See also: Hepatitis C; Liver; Virus

There are several types of hepatitis C, including genotype 1, which is the most common and accounts for approximately 70% of cases in the United States. Other genotypes include 2, 3, 4, 5, and 6. The symptoms of hepatitis C can range from mild to severe and may include fatigue, fever, loss of appetite, nausea, vomiting, joint pain, jaundice (yellowing of the skin and eyes), dark urine, pale stools, and itching all over the body. Some people with hepatitis C may not experience any symptoms at all.

Hepatitis C is diagnosed through a combination of blood tests that detect the presence of antibodies against HCV or the virus itself. Treatment typically involves a combination of medications, including interferon and ribavirin, which can cure the infection but may have side effects such as fatigue, nausea, and depression. In recent years, new drugs known as direct-acting antivirals (DAAs) have become available, which can cure the infection with fewer side effects and in a shorter period of time.

Prevention measures for hepatitis C include avoiding sharing needles or other drug paraphernalia, using condoms to prevent sexual transmission, and ensuring that any tattoos or piercings are performed with sterilized equipment. Vaccines are also available for people who are at high risk of contracting the virus, such as healthcare workers and individuals who engage in high-risk behaviors.

Overall, hepatitis C is a serious and common liver disease that can lead to significant health complications if left untreated. Fortunately, with advances in medical technology and treatment options, it is possible to manage and cure the virus with proper care and attention.

Necrosis is a type of cell death that occurs when cells are exposed to excessive stress, injury, or inflammation, leading to damage to the cell membrane and the release of cellular contents into the surrounding tissue. This can lead to the formation of gangrene, which is the death of body tissue due to lack of blood supply.

There are several types of necrosis, including:

1. Coagulative necrosis: This type of necrosis occurs when there is a lack of blood supply to the tissues, leading to the formation of a firm, white plaque on the surface of the affected area.
2. Liquefactive necrosis: This type of necrosis occurs when there is an infection or inflammation that causes the death of cells and the formation of pus.
3. Caseous necrosis: This type of necrosis occurs when there is a chronic infection, such as tuberculosis, and the affected tissue becomes soft and cheese-like.
4. Fat necrosis: This type of necrosis occurs when there is trauma to fatty tissue, leading to the formation of firm, yellowish nodules.
5. Necrotizing fasciitis: This is a severe and life-threatening form of necrosis that affects the skin and underlying tissues, often as a result of bacterial infection.

The diagnosis of necrosis is typically made through a combination of physical examination, imaging studies such as X-rays or CT scans, and laboratory tests such as biopsy. Treatment depends on the underlying cause of the necrosis and may include antibiotics, surgical debridement, or amputation in severe cases.

... may refer to: Alanine transaminase, an enzyme 4-aminobutyrate transaminase, an enzyme This set ...
Other names in common use include beta-alanine-pyruvate aminotransferase, and beta-alanine-alpha-alanine transaminase. This ... In enzymology, a beta-alanine-pyruvate transaminase (EC is an enzyme that catalyzes the chemical reaction L-alanine ... beta-alanine Thus, the two substrates of this enzyme are L-alanine and 3-oxopropanoate, whereas its two products are pyruvate ... HAYAISHI O, NISHIZUKA Y, TATIBANA M, TAKESHITA M, KUNO S (1961). "Enzymatic studies on the metabolism of beta-alanine". J. Biol ...
... beta-alanine ligase (AMP-forming). This enzyme participates in beta-alanine metabolism and pantothenate and CoA biosynthesis. ... Maas WK (1956). "Mechanism of the enzymatic synthesis of pantothenate from beta-alanine and pantoate". Fed. Proc. 15: 305-306. ... and beta-alanine, whereas its 3 products are AMP, diphosphate, and (R)-pantothenate. This enzyme belongs to the family of ... beta-alanine ligase (AMP-forming). Other names in common use include pantothenate synthetase, pantoate activating enzyme, ...
2010). "The cyanobacteria derived toxin beta-n-methylamino-L-alanine and Amyotrophic Lateral Sclerosis". Toxins. 2 (12): 2837- ... D. (1989). "Neurotoxicity of β -N-methylamino-L-alanine (BMAA) and β-N-oxalylamino-L-alanine (BOAA) on cultured cortical ... β-Methylamino-L-alanine, or BMAA, is a non-proteinogenic amino acid produced by cyanobacteria. BMAA is a neurotoxin and its ... BMAA is a derivative of the amino acid alanine with a methylamino group on the side chain. This non-proteinogenic amino acid is ...
The systematic name of this enzyme class is N-acetyl-beta-alanine amidohydrolase. This enzyme participates in beta-alanine ... beta-alanine Thus, the two substrates of this enzyme are N-acetyl-beta-alanine and H2O, whereas its two products are acetate ... a N-acetyl-beta-alanine deacetylase (EC is an enzyme that catalyzes the chemical reaction N-acetyl-beta-alanine + H2O ... Fujimoto D, Koyama T, Tamiya N (1968). "N-Acetyl-beta-alanine deacetylase in hog kidney". Biochim. Biophys. Acta. 167: 407-413 ...
... may refer to: Beta-pyrazolylalanine synthase, an enzyme Pyrazolylalanine synthase, an enzyme ...
4-phosphopantoate-beta-alanine+ligase at the US National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology ( ... beta-alanine ligase (AMP-forming). This enzyme catalyses the following chemical reaction ATP + (R)-4-phosphopantoate + β- ... 4-Phosphopantoate-β-alanine ligase (EC, phosphopantothenate synthetase, TK1686 protein) is an enzyme with systematic ... alanine ⇌ {\displaystyle \rightleftharpoons } AMP + diphosphate + (R)-4'-phosphopantothenate The conversion of (R)-pantoate to ...
... (or beta-alanine) is a naturally occurring beta amino acid, which is an amino acid in which the amino group is ... α-alanine). The IUPAC name for β-alanine is 3-aminopropanoic acid. Unlike its counterpart α-alanine, β-alanine has no ... beta-Alanine metabolism - Reference pathway". www.genome.jp. Retrieved 2016-10-04. KEGG map of β-alanine metabolism (CS1 maint ... histidine and β-alanine. Hence, by weight, only about 40% of the dose is available as β-alanine. Because β-alanine dipeptides ...
Wang, Yu; Xu, Huimin; White, Robert H. (August 2014). "Beta-alanine biosynthesis in Methanocaldococcus jannaschii". American ...
This enzyme participates in beta-alanine metabolism. It employs one cofactor, pyridoxal phosphate. Toyama S, Misono H, Soda K ( ...
This enzyme participates in beta-alanine metabolism. Nakamura K, Bernheim F (June 1961). "Studies on malonic semialdehyde ...
This enzyme participates in 4 metabolic pathways: inositol metabolism, alanine and aspartate metabolism, beta-alanine ... Hayaishi O, Nishizuka Y, Tatibana M, Takeshita M, Kuno S (March 1961). "Enzymatic studies on the metabolism of beta-alanine". ...
... also called N-carbamoyl-beta-alanine, is an intermediate in the metabolism of uracil. It is a urea derivative of beta-alanine ...
The beta-N-methylamino-L-alanine (BMAA) paradigm". Neurochemistry International. 50 (7): 998-1003. doi:10.1016/j.neuint.2006.12 ... The L-alanine derivative β-methylamino-L-alanine (BMAA) has long been identified as a neurotoxin which was first associated ... 2012). "Excitotoxic potential of the cyanotoxin β-methyl-amino-l-alanine (BMAA) in primary human neurons". Toxicon. 60 (6): ... that vervets orally administered BMAA developed hallmark histopathology features of Alzheimer's Disease including amyloid beta ...
Beta-alanine is a product of pyrimidine catabolism and histidine is an essential amino acid. Since beta-alanine is the limiting ... Carnosine (beta-alanyl-L-histidine) is a dipeptide molecule, made up of the amino acids beta-alanine and histidine. It is ... "beta-ureidopropionate + H2O => beta-alanine + NH4+ + CO2". reactome. Archived from the original on 2013-10-23. Retrieved 2020- ... Since beta-alanine is not incorporated into proteins, carnosine can be stored at relatively high concentrations (millimolar). ...
This enzyme participates in beta-alanine metabolism and propanoate metabolism. Den H, Robinson WG, Coon MJ (1959). "Enzymatic ... conversion of beta-hydroxypropionate to malonic semialdehyde". J. Biol. Chem. 234 (7): 1666-1671. PMID 13672942. Portal: ...
This enzyme participates in beta-alanine metabolism and propanoate metabolism. Hayaishi O (July 1955). "Enzymatic ...
In 2017, Bang Energy announced a caffeine-free variant of the beverage, using beta-alanine in place of caffeine. In 2019, the ... "Caffeine free Bang gets beta-alanine in place of caffeine". Stack3d. November 28, 2017. Archived from the original on May 16, ...
Beta-alanyl is an acyl group derived from beta-alanine. N2-beta-alanylarginine is a dipeptide of beta-alanine and arginine. ... Cytosolic non-specific dipeptidase is also known as N2-beta-alanylarginine dipeptidase glycyl-glycine dipeptidase glycyl- ...
Other names in common use include beta-(1-pyrazolyl)alanine synthase, beta-pyrazolealanine synthase, beta-pyrazolylalanine ... Murakoshi I, Ikegami F, Hinuma Y, Hanma Y (1984). "Purification and characterization of beta-(pyrazol-1-yl)-L-alanine synthase ... formation of beta-pyrazole-alanine by cloned cysteine synthase in vitro and in vivo". Biochem. Biophys. Res. Commun. 197 (3): ... "The enzymic synthesis of beta-substituted alanines". Phytochemistry. 11: 177-182. doi:10.1016/S0031-9422(00)89986-0. Noji M, ...
5. Enzymatic conversion of N-carbamyl-beta-alanine to beta-alanine, carbon dioxide, and ammonia". J. Biol. Chem. 235: 2375-8. ... beta-alanine + CO2 + NH3 Thus, the two substrates of this enzyme are N-carbamoyl-beta-alanine and H2O, whereas its 3 products ... In enzymology, a beta-ureidopropionase (EC is an enzyme that catalyzes the chemical reaction N-carbamoyl-beta-alanine ... CARAVACA J, GRISOLIA S (1958). "Enzymatic decarbamylation of carbamyl beta-alanine and carbamyl beta-aminoisobutyric acid". J. ...
BMAA is an abbreviation for the toxin beta-methylamino-L-alanine. BMAA may also refer to Baptist Missionary Association of ...
Beta-Alanine Creatine methyl ester Stout JR, Antonio J, Kalman E, eds. (2008). Essentials of Creatine in Sports and Health. ...
... is a derivative of non-proteinogenic amino acid beta-alanine. Lo, Wai Ling; Mok, Ka Leung; Yu ...
It also participates in beta-alanine metabolism and pantothenate and coa biosynthesis. The systematic name of this enzyme class ...
2004). "Identification of a G protein-coupled receptor specifically responsive to beta-alanine". J. Biol. Chem. 279 (22): 23559 ...
Murch SJ, Cox PA, Banack SA, Steele JC, Sacks OW (October 2004). "Occurrence of beta-methylamino-l-alanine (BMAA) in ALS/PDC ... namely the toxin beta-methylamino L-alanine (BMAA) from the cycad nut accumulating by biomagnification in the flying fox bat. ...
It migrates in beta-alanine-acetate-urea gel electrophoresis as a single compound. The phospholipase activity can be separated ...
beta-Methylamino-L-alanine Methyl-ONN-azoxymethanol beta-D-glucosyltransferase Carr, D.J.; Carr, S.G.M., eds. (1981). "The ...
In a 5 May BBC report, Cashman said that one of the toxins to be investigated was beta-Methylamino-L-alanine (BMAA), a ... Banack, SA; Caller, TA; Stommel, EW (2010). "The cyanobacteria derived toxin beta-n-methylamino-L-alanine and Amyotrophic ... Esterhuizen, M; Downing, TG (2008). "β-N-methylamino-L-alanine (BMAA) in novel South African cyanobacterial isolates". ... "Diverse taxa of cyanobacteria produce b-N-methylamino-L-alanine, a neurotoxic amino acid". PNAS. 102 (14): 5074-5078. Bibcode: ...
UMP synthesis from orotic acid or uridine and conversion of uracil to beta-alanine: enzymes and cDNAs. Progress in Nucleic Acid ...
... a derivative of amino acid beta-alanine), oil of lemon eucalyptus (OLE, a natural compound) and OLE's active ingredient para- ...
... beta-alanine + urea Thus, the two substrates of this enzyme are 3-guanidinopropanoate and H2O, whereas its two products are ... beta-alanine and urea. This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than ...
"The Arabidopsis thaliana isogene NIT4 and its orthologs in tobacco encode beta-cyano-L-alanine hydratase/nitrilase". The ... An example of this is the β-cyano-L-alanine nitrilase by the plant bacterium P. fluorescens SBW25. Although it is unknown ... ʟ-alanine. Other bacterial applications of nitrilases produced by plant-associated microorganisms include the degradation of ... those with high hydrolytic activity towards arylacetonitriles and those with high activity towards β-cyano-L-alanine. NIT1, 2, ...
As a member of the WNK family, the kinase's catalytic lysine residue is uniquely located in beta strand 2 of the glycine loop. ... Sterile20 related proline-alanine-rich kinase (SPAK) and oxidative stress response kinase 1 (OXSR1). Phosphorylation of SPAK's ...
House, William A.; Apgar, Jean; Smith, J. Cecil (1997-08-01). "The gerbil: A model for studying the metabolism of beta-carotene ... Apgar, J., Holley, R. W., & Merrill, S. H. (1962). "Purification of the alanine-, valine-, histidine-, and tyrosine-acceptor ... "Purification of the alanine-, valine-, histidine-, and tyrosine-acceptor ribonucleic acids from yeast" (1962, with Robert W. ... A model for studying the metabolism of beta-carotene and minerals" (1997, with William A. House and J. Cecil Smith) Jean ...
The core part of the domain is a 10 stranded beta barrel that is structurally similar to lipocalins and FABP. The N-terminal ... Logically, the histidine residues cannot be replaced by alanine in nature but this experimental replacement further confirms ... or by replacement of the histidine residues by alanine causes a large molecular motion of the bundle, separating the helices by ...
When taken with other supplements over a two-week period, such as beta-hydroxy beta-methylbutyrate (HMB), participants reported ... The degradation of L-leucine in the muscle to this compound allows for the production of the amino acids alanine and glutamate ... beta-hydroxy-beta-methylbutyrate (HMB)". Journal of the International Society of Sports Nutrition. 10 (1): 6. doi:10.1186/1550- ... beta-hydroxy-beta-methylbutyrate (HMB)". Journal of the International Society of Sports Nutrition. 10 (1): 6. doi:10.1186/1550- ...
... beta-2 microglobulin - beta adrenergic receptor - beta sheet - beta-1 adrenergic receptor - beta-2 adrenergic receptor - beta- ... leucine-2-alanine enkephalin - leukotriene B4 receptor - LH - LH receptor - LHRH receptor - life - life form - ligand - light ... transforming growth factor beta - transforming growth factor beta receptor - transient receptor potential - translation ( ... alpha-beta T-cell antigen receptor - alpha-fetoprotein - alpha-globulin - alpha-macroglobulin - alpha-MSH - Ames test - amide ...
The heavy fibroin protein consists of layers of antiparallel beta sheets. Its primary structure mainly consists of the ... recurrent amino acid sequence (Gly-Ser-Gly-Ala-Gly-Ala)n. The high glycine (and, to a lesser extent, alanine) content allows ...
The only differences are two amino-acid substitutions at positions 8 and 34, where alanine and lysine are replaced by 2- ... It appears to enhance growth of pancreatic beta cells, which are responsible for insulin production and release. It also ...
UDP-N-acetylmuramate-L-alanine ligase, DUF2236 domain-containing protein, cobaltochelatase subunit CobN, alpha/beta hydrolase, ...
The non-proteinogenic amino acid beta-Methylamino-L-alanine (BMAA) is ubiquitously produced by cyanobacteria in marine, ... Weiss JH, Koh JY, Choi DW (1989). "Neurotoxicity of β -N-methylamino-L-alanine (BMAA) and β-N-oxalylamino-L-alanine (BOAA) on ... 2008). "β-N-methylamino-L-alanine (BMAA) in novel South African cyanobacterial isolates". Ecotoxicology and Environmental ... 2007). "β-N-methylamino-L-alanine enhances neurotoxicity through multiple mechanisms". Neurobiology of Disease. 25 (2): 360-366 ...
This is due to the fact that the beta oxidation of long chain fatty acids with an odd number of carbons produces propionyl-CoA ... beginning with a methionine and ending with an alanine). The polypeptide chain in the mature protein is comprised between amino ... which is produced by the peroxisomal beta oxidation of odd chain length dicarboxylic fatty acids (odd chain length DFAs). While ... "Cloning and expression of rat pancreatic beta-cell malonyl-CoA decarboxylase". The Biochemical Journal. 340 (1): 213-7. doi: ...
Holtzer ME, Kidd SG, Crimmins DL, Holtzer A (Mar 1992). "Beta beta homodimers exist in native rabbit skeletal muscle ... Mouse transgenic studies in which the phosphorylation site in α-tropomyosin is mutated to Alanine have shown that ... Monnier N, Lunardi J, Marty I, Mezin P, Labarre-Vila A, Dieterich K, Jouk PS (Feb 2009). "Absence of beta-tropomyosin is a new ... β-Tropomyosin, also known as tropomyosin beta chain is a protein that in humans is encoded by the TPM2 gene. β-tropomyosin is ...
... these include poly-leucine and poly-alanine. Both poly-L- and poly-D-amino acids are available and cause the opposite ... beta-unsaturated ketones catalyzed by silica-grafted poly-(L)-leucine catalysts". Tetrahedron Lett. 2005, 46 (34), 5665-5668. ... alanine] System". Angewandte Chemie International Edition in English. 19 (11): 929. doi:10.1002/anie.198009291. Juliá, ...
The phenylalanine of the ball interacts with the alanine in domain III's S4-S5 segments and the asparagine in domain IV's S4-S5 ... Xia XM, Ding JP, Lingle CJ (2003). "Inactivation of BK Channels by the NH2 Terminus of the beta Auxiliary Subunit An Essential ... "The human heart and rat brain IIA Na+ channels interact with different molecular regions of the beta subunit". The Journal of ...
It is caused by a different toxin (beta-aminopropionitrile) which affects the linking of collagen, a protein of connective ... also known as β-N-oxalyl-amino-L-alanine, or BOAA) causes paralysis, characterized by lack of strength in or inability to move ... The cause of this disease is attributed to beta-aminopropionitrile, which inhibits the copper-containing enzyme lysyl oxidase, ... It is a skeletal disorder, caused by the toxin beta-aminopropionitrile (BAPN), and characterized by hernias, aortic dissection ...
After his army service, Schellman used his G.I. Bill benefits and completed an A.B at Temple University, Phi Beta Kappa, in ... "Large differences in the helix propensities of alanine and glycine". Nature. 351 (6327): 586-588. doi:10.1038/351586a0. ISSN ...
Elastases form a subfamily of serine proteases, characterized by a distinctive structure consisting of two beta barrel domains ... isoleucine and alanine. The wide specificity of elastases for non-aromatic uncharged side chains can explain its ability to ...
Hsu YC, Tai DI (2011). "Unusually high alanine aminotransferase to aspartate aminotransferase ratio in a patient with ... Spona J, Lunglmayr G (July 1980). "Prolaktin-Serumspiegel unter Behandlung des Prostatakarzinoms mit Östradiol-17 beta- ... Serum Prolactin Levels During Therapy of Prostatic Cancer with Estradiol-17 beta-undecylate and Cyproterone Acetate]. Wien. ...
Other names in common use include beta-(3,4-dihydroxyphenyl)-L-alanine (DOPA) ammonia-lyase, and 3,4-dihydroxy-L-phenylalanine ...
Members of the epithelial Na+ channel (ENaC) family fall into four subfamilies, termed alpha, beta, gamma and delta. The ... subunit by alanine mutagenesis". American Journal of Physiology. Renal Physiology. 300 (4): F887-97. doi:10.1152/ajprenal. ... "Gene structure of the human amiloride-sensitive epithelial sodium channel beta subunit". Biochemical and Biophysical Research ...
This causes an alanine to valine residue substitution at amino acid position 114, a location highly conserved in all organisms ... "The Wnt receptor FZD1 mediates chemoresistance in neuroblastoma through activation of the Wnt/beta-catenin pathway". Oncogene. ... "Expression of Wnt4 in human pituitary adenomas regulates activation of the beta-catenin-independent pathway". Endocrine ...
... and beta-ergocryptine. Ergotoxine group (valine as the amino acid attached to the ergoline moiety, at R2 below) Ergocristine ... alanine at R2) Ergotamine IUPAC name: Ergotaman-3',6',18-trione, 12'-hydroxy-2'-methyl-5'-(phenylmethyl)-, (5'-alpha)- CAS ... 561-94-4 beta-Ergosine IUPAC name: Ergotaman-3',6',18-trione, 12'-hydroxy-2'-methyl-5'-(1-methylpropyl)-, (5'-alpha(S))- CAS ... 511-09-1 beta-Ergocryptine IUPAC name: Ergotaman-3',6',18-trione, 12'-hydroxy-2'-(1-methylethyl)-5'-(1-methylpropyl)-, (5'alpha ...
From the middle stage until term, the beta cells continue to increase in number until they reach an approximate 1:1 ratio with ... However, a study of an infusion of alanine into pregnant women was shown to increase the cord blood and maternal glucagon ... Five weeks later, the pancreatic alpha and beta cells have begun to emerge. Reaching eight to ten weeks into development, the ... As such, while the fetal pancreatic alpha and beta islet cells have fully developed and are capable of hormone synthesis during ...
Two hydrophobic loops contain conserved asparagine-proline-alanine ("NPA motif") which form a barrel surrounding a central pore ... Beta vulgaris L.) involved in boron homeostasis and abiotic stress". Plant, Cell & Environment. 41 (12): 2844-2857. doi:10.1111 ... with an asparagine-proline-alanine ("NPA motif") pattern. They create a distinctive hourglass shape, making the water channel ...
... assembly of a novel active site in Flp recombinase harboring alanine at this position". Journal of Molecular Biology. 368 (1): ... a heat shock promoter to induce the production of FLP while a FRT-flanked vector separated the CaMV 35S promoter from the beta- ...
Female masters athletes might get more of a boost than other athletes from beta-alanine supplements. ... Beta-alanine has been shown to have a beneficial effect on exercise in some studies, but not in others. Glenn and his ... Beta-alanine, a nonessential amino acid, appears to function as a precursor to carnosine in muscle tissue. Carnosine buffers ... However, he said, "there are a lot of really good data that indicate that 3.2 g of beta-alanine is enough to significantly ...
Testing Status of beta-Alanine M040009. Testing Status of beta-Alanine M040009. CASRN: 107-95-9. Formula: C3-H7-N-O2. Synonyms/ ...
In two siblings with a complete DHP deficiency and a variable clinical presentation, a normal concentration of beta-alanine and ... Beta-alanine and beta-aminoisobutyric acid levels in two siblings with dihydropyrimidinase deficiency A B P van Kuilenburg 1 , ... Beta-alanine and beta-aminoisobutyric acid levels in two siblings with dihydropyrimidinase deficiency A B P van Kuilenburg et ... a normal concentration of beta-alanine and strongly decreased levels of beta-aminoisobutyric acid were observed in plasma, ...
Genetic Toxicity Evaluation of beta-Alanine in Salmonella/E.coli Mutagenicity Test or Ames Test. Study A27555 Summary Data. * ... beta-Alanine (107-95-9). Chemical Effects in Biological Systems (CEBS). Research Triangle Park, NC (USA): National Toxicology ... An overview of Genetic Toxicology Bacterial Mutagenicity study conclusions related to beta-Alanine (107-95-9). Bacterial ... Home » Chemical Effects in Biological Systems (CEBS) » beta-Alanine (107-95-9) ...
Beta-alanine:. *Children: 0 to 49. *Adults: 0 to 29. Beta-amino-isobutyric acid:. *Children: not detected ...
Ogfod1 deletion increases cardiac beta-alanine levels and protects mice against ischemia-reperfusion injury. ...
beta-Alanine metabolism. 28. 13. 9.. 8. e. −. 4. 0.38. Phenylalanine metabolism. 45. 18. 9.. 9. e. −. 4. 0.45. ... Alanine, aspartate, and glutamate metabolism. 24. 13. 1.. 4. e. −. 4. 0.88. ...
Beta-alanine. Beta-alanine. Beta-alanine is an amino acid in foods such as meat, poultry, and fish. People get up to about 1 ... Whether beta-alanine helps with endurance activities like cycling isnt clear. Its also not clear whether beta-alanine mainly ... Beta-hydroxy-beta-methylbutyrate (HMB). Beta-hydroxy-beta-methylbutyrate (HMB). Your body converts a small amount of leucine, ... gram a day of beta-alanine, depending on their diet. Your body uses beta-alanine to make carnosine in skeletal muscles. When ...
"β-N-methylamino-l-alanine (L-BMAA) is produced by cyanobacteria (blue-green algae). Human exposure to L-BMAA occurs via ... beta-N-methylamino-L-alanine Actions. * Search in PubMed * Search in MeSH ... Disposition of β-N-methylamino-l-alanine (L-BMAA), a neurotoxin, in rodents following a single or repeated oral exposure ... Disposition of β-N-methylamino-l-alanine (L-BMAA), a neurotoxin, in rodents following a single or repeated oral exposure ...
Cycasin and beta-N -methyl-amino-L-alanine (BMAA) are putative neurotoxins in the seed. If the seeds are repeatedly washed, ... Unlike in Alzheimers disease, no beta-amyloid deposits are seen in PSP. Tau protein abnormalities have also been found in ... form has both Lewy bodies and Alzheimers type neuritic amyloid-beta protein containing plaques and tau-protein containing ...
Cyanobacterial blooms and the occurrence of the neurotoxin beta-n-methylamino-l-alanine (BMAA) in south Florida aquatic food ... Reply to "Lack of beta-methylamino-L-Alanine in brain from controls, AD, or Chamorros with PDC". Neurology ... Diverse taxa of cyanobacteria produce b-N-methylamino-L-alanine, a neurotoxic amino acid. Proc Natl Acad Sci USA 102: 5074-5078 ...
7. Beta-alanine suppresses heat inactivation of lactate dehydrogenase.. Mehta AD; Seidler NW. J Enzyme Inhib Med Chem; 2005 Apr ... 1. β-Alanine intercede metabolic recovery for amelioration of human cervical and renal tumors.. Pandurangan M; Enkhtaivan G; ... 6. Carnosine and anserine homeostasis in skeletal muscle and heart is controlled by β-alanine transamination.. Blancquaert L; ...
INTERFERON BETA-1B (UNII: TTD90R31WZ) (INTERFERON BETA-1B - UNII:TTD90R31WZ) INTERFERON BETA-1B. 0.25 mg in 1 mL. ... Alanine aminotransferase increased. (SGPT , 5 times baseline) 4%. 12%. Aspartate aminotransferase increased. (SGOT , 5 times ... interferon beta-1b (in-ter-feer-on beta-one-be). Read the Instructions for Use that come with your BETASERON before you start ... Interferon beta-1b is a purified, sterile, lyophilized protein product produced by recombinant DNA techniques. Interferon beta- ...
... and beta-methylamino-l-alanine in human urineExternal. Bhandari D, Bowman BA, Patel AB, Chambers DM, De Jesus VR, Blount BC.. J ... beta-methylamino-l-alanine (BMAA), and trimethylamine N-oxide (TMAO), in human urine. Urinary aliphatic diamines, HDA and IPDA ... HEV RNA was detected from 2 to 24 days after inoculation (DAI) in stool and serum, elevated alanine aminotransferase (ALT) ...
juice, Beta-alanine, Beta-hydroxy-beta-methylbutyrate, HMB, Betaine,Branched-chain amino acids ,BCAAs, Caffeine, Citrulline, ...
Studies that investigate biologically active compounds, e.g., beta-Methylamine alanine (BMAA) a potent neuroxtoxin, or other ...
And much to my chagrin, I found that ammonia added across the double bond to form a beta alanine as a product. But anyway, as a ...
This protein may also function as a beta-alanine carrier. Mutations in this gene may be associated with X-linked obesity. A ...
Summary: Pantothenate synthase; also known as pantoate-beta-alanine ligase, required for pantothenic acid biosynthesis, ...
Three pathways were significantly perturbed in exposed workers and had an impact score >0.5: beta-alanine metabolism, histidine ... beta-alanine, methionine, n-isovalerylglycine, and threonine. ...
Beta Alanine. 5.00 out of 5. 159.00 Kn * VBR energy shot 60 mL. 5.00 out of 5 ...
The transporter is specific for taurine and other beta-amino acids, including beta-alanine, and exhibits high affinity for ...
Substitution of alanine for aspartate at position 179 in the SHV-6 extended-spectrum beta-lactamase. FEMS Microbiol Lett. 1997; ... Ho PL, Poon WW, Loke SL, Leung MS, Chow KH, Wong RC, Community emergence of CTX-M type extended-spectrum beta-lactamases among ... Colodner R, Rock W, Chazan B, Keller N, Guy N, Sakran W, Risk factors for the development of extended-spectrum beta-lactamase- ... Saladin M, Cao VT, Lambert T, Donay JL, Herrmann JL, Ould-Hocine Z, Diversity of CTX-M beta-lactamases and their promoter ...
BETA.-ALANINE. .BETA.-ALANINE. Unique Ingredient Identifier (UNII). Drug Active Ingredients. Details. ... BETA.-CITRONELLOL, R-(+)-. .BETA.-CITRONELLOL, R-(+)-. Unique Ingredient Identifier (UNII). Drug Active Ingredients. Details. ... BETA.-D.-FRUCTOFURANOSE. .BETA.-D.-FRUCTOFURANOSE. Unique Ingredient Identifier (UNII). Drug Active Ingredients. Details. ... BETA.-D-FRUCTOPYRANOSE. .BETA.-D-FRUCTOPYRANOSE. Unique Ingredient Identifier (UNII). Drug Active Ingredients. Details. ...
... alanine, glutamic acid and glycine, beta-sitosterol, lycopene, nettle root extract, quercitin, Belizian Man Vine extract, mulra ...
beta-Alanine Hydrochloride beta-Alanine, Calcium Salt (2:1) beta-Alanine, Monopotassium Salt beta-Alanine, Monosodium Salt ... beta-Alanine, Monosodium Salt Narrower Concept UI. M0329502. Registry Number. 16690-93-0. Terms. beta-Alanine, Monosodium Salt ... beta-Alanine, Calcium Salt (2:1) Narrower Concept UI. M0329503. Registry Number. 36321-40-1. Terms. beta-Alanine, Calcium Salt ... beta-Alanine Hydrochloride Narrower Concept UI. M0329505. Registry Number. 6057-90-5. Terms. beta-Alanine Hydrochloride ...
beta-Alanine - Pyruvate Transaminase beta-Alanine Pyruvate Aminotransferase Registry Number. EC Public MeSH Note. ... beta-Alanine-Pyruvate Transaminase Preferred Term Term UI T636788. Date04/14/2005. LexicalTag NON. ThesaurusID NLM (2006). ... beta-Alanine-Pyruvate Transaminase Preferred Concept UI. M0079278. Registry Number. EC Scope Note. A PYRIDOXAL ... beta-Alanine - Pyruvate Transaminase Term UI T109281. LexicalTag NON. ThesaurusID NLM (2006). ...
  • Increasing carnosine levels through Beta Alanine supplementation may delay fatigue during endurance exercise or translate into lifting more weights and increasing total work output. (lky7sports.com)
  • One study looked at the effect of beta-alanine supplementation and muscle carnosine concentrations on the performance of highly trained rowers. (clubvits.com)
  • Before supplementation the placebo group was 0.3 seconds quicker, however after the supplementation those taking beta-alanine were 4.3 seconds quicker. (clubvits.com)
  • A study using 400m sprint trained athletes found that beta-alanine supplementation significantly increased muscle carnosine levels. (clubvits.com)
  • The real benefit is experienced following several weeks of daily supplementation as it takes time to build up and saturate your muscles beta-alanine stores. (clubvits.com)
  • β-Alanine supplementation augments muscle carnosine content and attenuates fatigue during repeated isokinetic contraction bouts in trained sprinters. (clubvits.com)
  • Clinical studies suggest that Beta-Alanine supplementation can help delay muscle fatigue for increased endurance during exercise. (vitaminherbstore.com)
  • After a few weeks of supplementation with Beta-Alanine, this sensation normally lessens or subsides. (vitaminherbstore.com)
  • Research studies have shown that Beta-Alanine supplementation not only can boost performance but also support increases in lean muscle mass. (monsterzym.com)
  • Beta-alanine supplementation has become popular in recent years, as it is thought to increase muscle carnosine levels and improve exercise performance. (supplementsguide.co)
  • However, one of the side effects of beta-alanine supplementation is a condition known as paresthesia, which is characterized by a tingling or prickling sensation on the skin. (supplementsguide.co)
  • While the tingling sensation caused by beta-alanine supplementation may be uncomfortable for some, it is generally harmless and will subside once supplementation is stopped. (supplementsguide.co)
  • The good news is that the beta-alanine itch is generally harmless and will subside once supplementation is stopped. (supplementsguide.co)
  • If you're new to beta-alanine supplementation, it's best to start with a lower dose and increase it gradually over time. (supplementsguide.co)
  • The most common side effect of beta-alanine supplementation is the beta-alanine itch, which is a tingling or prickling sensation on the skin. (supplementsguide.co)
  • Beta-Alanine supplementation can increase muscle Carnosine content and delay muscle fatigue. (fitshop.ca)
  • Taking beta-alanine won't increase your 1RM or how much you can bench press. (bodybuilding.com)
  • The best way to get the carnosine you need is by taking beta-alanine. (bodybuilding.com)
  • Taking Beta-Alanine can fight off these hydrogen ions. (preworkoutbuzz.com)
  • Beta-alanine is a nonessential beta-amino acid that increases muscle carnosine levels. (bodybuilding.com)
  • They found that the carnosine levels in the calf muscles of those who had taken beta-alanine had increased significantly. (clubvits.com)
  • The neurotoxin β-N-methylamino-L-alanine (BMAA), a non-proteinogenic amino acid produced by several species of both prokaryotic (cyanobacteria) and eukaryotic (diatoms) microorganisms, has been proposed to be associated with the development of neurodegenerative diseases. (mdpi.com)
  • Beta-Alanine is an amino acid which has become very popular in the world of sports nutrition as research has shown that it improves muscular endurance. (clubvits.com)
  • When ingested beta alanine binds with the amino acid histidine to produce an acidity buffer known as Carnosine. (clubvits.com)
  • The chemical reactions and pathways resulting in the breakdown of beta-alanine (3-aminopropanoic acid), an achiral amino acid and an isomer of alanine. (tamu.edu)
  • Beta-Alanine is a non-essential amino acid naturally produced in muscle cells. (vitaminherbstore.com)
  • Beta-alanine is a naturally occurring amino acid that is classified as a non-essential amino acid. (supplementsguide.co)
  • Tested Beta Alanine is a non-essential amino acid that is converted to carnosine by the muscle cells. (fitshop.ca)
  • Since neuronal uptake and neuronal receptor sensitivity to beta-alanine have been demonstrated, the compound may be a false transmitter replacing GAMMA-AMINOBUTYRIC ACID. (nih.gov)
  • The results of studies on beta-alanine, an amino acid found in food and dietary supplements, are mixed but generally don't show that it improves athletic performance significantly. (nih.gov)
  • Along with creatine, BCAA's and caffeine, beta-alanine has become a staple of pre-workout supplements. (clubvits.com)
  • Although beta-alanine is often taken before training and is incorporated into many pre-workout supplements it can be taken at any time throughout the day. (clubvits.com)
  • Beta Alanine_Dietary supplements ingredients, vitamins and minerals. (health-sources.com)
  • pouze od takov ch u ivatel , kte v na em obchod Beta Alanine 1000 zakoupili a pot k n mu napsali recenzi. (ronnie.cz)
  • Amino acids are the building blocks of proteins, and beta-alanine is used by muscles to synthesize carnosine. (supplementsguide.co)
  • As a byproduct, beta alanine can also decrease fatigue while training and increase total workload. (elitefts.com)
  • Research suggests that supplementing with 4-6 grams of beta-alanine daily for 28 days can lead to a 40-60 percent increase in carnosine concentrations. (bodybuilding.com)
  • If you're not a fan of the tingling sensation you can get when you take larger doses of beta-alanine, split them into smaller doses of 1.6 grams. (bodybuilding.com)
  • The recommended dosage of beta-alanine is 2-5 grams per day. (supplementsguide.co)
  • In fact, the typical dose of beta-alanine used in most pre-workouts is far too little to have any immediate effect on performance, which is why you have to take it every day and give it time to build up inside your system. (bodybuilding.com)
  • The standard daily dose of beta-alanine is between 3-6 g. (clubvits.com)
  • Olimp Beta-alanine Carno Rush Mega Tabs ® - a specially-designed combination of beta-alanine, l-histidine and vitamin B6! (beingbuilder.com)
  • Beta-alanine and L-histidine supplemented together provide two substances necessary for the synthesis of carnosine, which shows great anti-oxidizing potential and may delay degrading processes in the cells during intense workouts. (beingbuilder.com)
  • Three pathways were significantly perturbed in exposed workers and had an impact score >0.5: beta-alanine metabolism, histidine metabolism, and glycine, serine, and threonine metabolism. (cdc.gov)
  • 5. Brown adipose tissue transcriptome unveils an important role of the Beta-alanine/alamandine receptor, MrgD, in metabolism. (nih.gov)
  • Al haberse demostrado la captación neuronal y la sensibilidad receptora neuronal a la beta-alanina, el compuesto puede ser un transmisor falso, sustituto del ÁCIDO GAMMA AMINOBUTÍRICO. (bvsalud.org)
  • Beta-Alanine may cause a harmless, temporary tingling sensation on the skin for some individuals. (vitaminherbstore.com)
  • Food sources such as beef and chicken contain beta-alanine however only in small doses. (clubvits.com)
  • Some companies may put a gram or two of beta-alanine into pre-workouts just to give you an instant physical sensation. (bodybuilding.com)
  • When levels of beta-alanine and carnosine become too high, they begin to interact with nerve endings in the skin, causing the tingling sensation. (supplementsguide.co)
  • Boost your performance by learning how to supplement with beta-alanine the right way! (bodybuilding.com)
  • If you're going to supplement with beta-alanine, here's what you need to know about this widely used, but poorly understood, ingredient. (bodybuilding.com)
  • The availability of beta-alanine is the limiting factor when it comes to carnosine production therefore taking it in supplement form will allow more carnosine to be formed. (clubvits.com)
  • Olimp Beta-alanine Carno Rush Mega Tabs® is a supplement designed for all who practice strength-endurance sports, strength sports and endurance sports that require great physical fitness mai. (beingbuilder.com)
  • Olimp Beta-alanine Carno Rush Mega Tabs ® is a supplement designed for all who practice strength-endurance sports, strength sports and endurance sports that require great physical fitness maintained for a longer period of time, or have a great frequency of training sessions. (beingbuilder.com)
  • Additionally, beta-alanine has been shown to be a safe and effective supplement for improving exercise performance. (supplementsguide.co)
  • So, if you're looking for a supplement that can help you train harder and longer, beta-alanine may be a good option for you. (supplementsguide.co)
  • If you've ever taken a beta-alanine supplement, chances are you've experienced the "beta-alanine itch. (supplementsguide.co)
  • This will help your body to adjust to the supplement and minimize the chances of experiencing the beta-alanine itch. (supplementsguide.co)
  • Creatine's ability to improve high-intensity exercise makes it a perfect complement to beta-alanine's ability to help you extend your workouts. (bodybuilding.com)
  • Tested Beta Alanine can improve muscular endurance and performance during high intensity exercise. (fitshop.ca)
  • 18 rowers supplemented with 5g/day of either a placebo or beta-alanine for 7 weeks. (clubvits.com)
  • This increase in acidity impairs the muscles ability to contract with force… this is where beta-alanine comes in. (clubvits.com)
  • In fact, a 2017 survey of 570 athletes who took beta-alanine found that 65 percent of them couldn't identify its benefits , and only 12 percent took it every day as recommended. (bodybuilding.com)
  • Buy Tested Nutrition Beta-Alanine (180 Caps) for Less! (fitshop.ca)
  • Ogfod1 deletion increases cardiac beta-alanine levels and protects mice against ischemia-reperfusion injury. (nih.gov)
  • In one study, athletes who consumed both creatine and beta-alanine demonstrated better endurance than those who took only one. (bodybuilding.com)
  • A second study found that athletes who followed a 10-week resistance-training program and supplemented with creatine and beta-alanine saw greater improvements in muscle mass and body fat. (bodybuilding.com)
  • Beta-alanine is one of those ingredients that seems to find its way into just about every pre-workout on the market. (bodybuilding.com)
  • Olimp Beta-alanine Carno Rush Mega Tabs ® helps to prolong the time before becoming tired, thus increasing the workout volume significantly. (beingbuilder.com)
  • Beta Alanine is ideal for anyone participating in explosive sports (such as weightlifting) or those involved in prolonged endurance exercise. (lky7sports.com)
  • 1] Most of the athletes also grossly underestimated the time required for beta-alanine to take effect. (bodybuilding.com)
  • Or you can choose products with the sustained-release form of beta-alanine, which has the same effect of increasing carnosine stores, but with little or no tingling. (bodybuilding.com)
  • Cases of pulmonary arterial hypertension (PAH) have been reported in patients treated with interferon beta products, including EXTAVIA. (nih.gov)
  • The exact mechanism by which beta-alanine causes paresthesia is not fully understood, but it is thought to be due to the accumulation of beta-alanine and carnosine in the bloodstream. (supplementsguide.co)
  • This side effect is caused by the accumulation of beta-alanine and carnosine in the bloodstream. (supplementsguide.co)
  • PrimaForce™ Beta-Alanine helps users train harder for longer. (monsterzym.com)